DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Note: the application has been transferred to Examiner Wayne Zhong. Any inconvenience is apologized.
Status of claims
Applicant’s response filed 4/22/2026 has been entered.
Claims 2-7, 9-11, 13-14, 16-21, 23, 25-29, 31-33, 35-49, 51-55, 58-59, 63-83 had/have been canceled by the applicant.
Claims 1, 8, 22, 50, 86 have been amended.
In summary, claims 1, 8, 12, 15, 22, 24, 30, 34, 50, 56-57, 60-62, 84-86 are pending and examined in this office action.
All previous objections and rejections not set forth below have been withdrawn in view of the applicant’s amendment and/or upon further consideration. See “Response to Arguments” at the end of office action.
The following rejections are repeated, modified and/or added for the reasons of record as set forth in the last Office action of 1/23/2026, and/or necessitated by the applicant’s amendments. The applicant’s arguments filed 4/22/2026 have been thoroughly considered but are not deemed fully persuasive.
Claim Objections
Claim 24 is objected to because of the following informality:
In (f), last line, a “;” should be inserted: the “(LOX3) and/or” should be ---(LOX3); and/or---.
See the requirement of 37 CFR 1.71(a) for “full, clear, and exact terms”.
Appropriate correction is required.
Claim Rejections - 35 USC § 103
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
The factual inquiries set forth in Graham v. John Deere Co., 383 U.S. 1, 148 USPQ 459 (1966), that are applied for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or non-obviousness.
Claims 1, 8, 12, 22, 30, 50, 56-57, 60-61, 84 are rejected under 35 U.S.C. 103 as being unpatentable over Gao et al Disruption of a Maize 9-Lipoxygenase Results in Increased Resistance to Fungal Pathogens and Reduced Levels of Contamination with Mycotoxin Fumonisin. MPMI, p922–933, 2007), in view of Kim et al (Genomic DNA of lipoxygenase gene, Q8W0V2_MAIZE, 3/1/2002), and Qi et al (High-efficiency CRISPR/Cas9 multiplex gene editing using the glycine tRNA-processing system-based strategy in maize. BMC Biotechnology, p1-8, 2016).
Amended independent claim 1 is drawn to a maize plant or plant part thereof comprising at least one deletion mutation in at least one endogenous Lipoxygenase (LOX) gene encoding a LOX protein,
wherein the at least one endogenous LOX gene comprises a sequence encoding a sequence having at least 95% identity to any one of the amino acid sequences of SEQ ID NOs: 74, 77, 80, or 83, and
wherein the maize plant comprising the at least one mutation exhibits increased resistance to ear rot and/or stalk rot compared to a maize plant devoid of the at least one mutation.
Claim 8 limits claim 1, wherein the at least one mutation in the at least one endogenous LOX gene results in a truncated protein.
Amended independent claim 22 is drawn to a maize plant cell comprising at least one mutation (where in the mutation reduces expression of the LOX gene in the maize plant cell or the LOX gene comprising the at least one mutation encodes a truncated protein) within a LOX gene that results in a null allele or knockout of the LOX gene,
wherein the at least one mutation is a base substitution, a base insertion or a base deletion that is introduced using an editing system that comprises a nucleic acid binding domain that binds to a target site in the LOX gene,
wherein the LOX gene comprises a coding sequence that encodes a sequence having at least 95% sequence identity to any one of the amino acid sequences of SEQ ID NOs:74, 77, 80, or 83.
Amended independent claim 50 is drawn to a method comprising contacting a target site in the endogenous LOX gene in the maize plant or plant part thereof with a nuclease comprising a cleavage domain and a nucleic acid binding domain, wherein the nucleic acid binding domain binds to the target site in the endogenous LOX gene, wherein the endogenous LOX gene encodes a sequence having at least 95% sequence identity to any one of the amino acid sequences of SEQ ID NOs:74, 77, 80, or 83, thereby producing the maize plant or plant part thereof comprising the endogenous LOX gene having the mutation and exhibiting increased resistance to ear rot and/or stalk rot,
for producing a maize plant or plant part thereof comprising an endogenous LOX gene having a mutation and increased resistance to ear rot and/or stalk rot (preamble).
Claim 56 limits claim 50, wherein the mutation is a deletion.
Claim 57 limits claim 56, wherein the deletion results in a truncation.
Regarding claims 1, 8, 22, 50 and 56-57
Gao et al teach a knockout of maize LOX3 into exon 5 of the endogenous Maize LOX3 gene allele lox3-4 on page 923 (see 1ox3-4 exon V insertion in fig 1A) that knocked out LOX3 gene expression (see page 923 in figure 1D) by deleting the message, truncated the encoded LOX3 protein open reading frame that resulted in increased resistance to stem rot and root rot as a reduction of the disease severity upon F. verticillioides, Colletotrichum graminicola, and Cochliobolus heterostrophus infections (see page 928 in figure 6A and 6B; and page 929 sentence spanning left and right column).
Gao et al teach the method of producing such maize plant or part or cell (“Materials and Methods” in p930-931) and the resultant maize plant or part or cell (“Results” in p924-928). Gao et al demonstrated the increased resistance to stalk rots (p922, Abstract; p926, right col, 3rd para; p929, left col, 2nd para).
The steps of generation of LOX3 mutant in the “Materials and Methods” (p930, right col, last para; p931, left col, 1st para) reads on “contacting a target site in the endogenous LOX gene in the maize plant or plant part thereof with a nuclease comprising a cleavage domain and a nucleic acid binding domain, wherein the nucleic acid binding domain binds to the target site in the endogenous LOX gene, wherein the endogenous LOX gene” of claim 50.
Thus, Gao et al teach the limitation of claims and demonstrated the success thereof, except are silent that the LOX3 sequence is SEQ ID NO: 80, and do not teach the mutation is a deletion mutation.
Kim et al teach (disclose and characterize) a LOX3 sequence from maize 100% identical to instant SEQ ID NO: 80, and the Genomic DNA of lipoxygenase gene. See “Sequence Matches” at the end of office action.
Thus, either the LOX3 sequence of Gao et al is SEQ ID NO: 80, or at the very least it is a LOX3 polymorphism of SEQ ID NO: 80, thus one ordinary skill in the art would have been motivated to knockout such a sequence by using the method as taught by Gao et al.
Using deletion for gene knockout is a routine technique as insertion is.
For example, Qi et al teach a technique of editing maize genes and/or deletions, also commonly called indels (p4, fig 2; p5, fig 3), including knock-out maize genes (p7, whole page).
Qi et al specifically tech and demonstrated the success of using fragment deletion for maize gene editing (p1, Abstract; p2, left col, 2nd to 3rd para; p5, whole right col, fig 3).
Qi particularly demonstrated that insertion or deletion or the combination of both resulted in maize gene editing including truncation of fragments (p5, fig 3).
In addition, the applicant admits that “other types of mutations useful for production of plants exhibiting increased resistance to ear rot and/or stalk rot include substitutions, deletions and insertions” (p40, 3rd para), and that “the edit results in a non-naturally occurring mutation, including but not limited to a deletion, substitution, or insertion, wherein the edit may result in a null allele or in a dominant negative mutation (p45, 3rd para).
Thus, by the teaching of prior art like Qi et al, and by the applicant’s own admission, deletion and substitution or insertion are functional equivalents in term of producing a gene editing, including a dominant negative mutation and increased resistance to ear rot and/or stalk rot.
Regarding dependent claims, Gao et al teach that LOX3-1, LOX3-2, LOX3-3 and LOX3-4 are mutated and knocked out (p924, left col, 2nd para), the limitation of claims 12 and 61.
Gao et al teach that the plant cell is growing into a plant comprising the at least one mutation and exhibiting increased resistance to stalk rot compared to a wild-type maize plant without the mutation (p26, fig 4), the limitation of claims 30 and 34.
As analyzed above, Gao et al teach LOX gene knockout (p924, right col, 1st para, fig 2). Qi et al teach making deletion mutations. Hence, making deletions of at least 3 consecutive bases from 3’ end would truncate nearly all of the transcription. Hence, Gao et al and Qi et al collectively provide teaching and motivation for one ordinary skill in the art to delete at least 3 consecutive bases from 3’ end of the LOX gene, the limitation of claim 60.
Qi teach that the deletions are clearly more than 3 base pairs but less than 200 base pairs (p5, fig 3, B and C), the limitation of claim 84.
An invention would have been obvious to one ordinary skill in the art if any teaching, suggestion or motivation in prior art leading the one to combine the teaching(s) or suggestion(s) of the cited references to arrive the claimed invention.
In this case, it would have been obvious for one ordinary skill in the art to modify the invention of Gao et al, such that the knockout of LOX as taught by Gao et al is using the technique of deletion mutation to substitute or as an alternative of Gao et al, for maize editing and knockout, as taught by Qi et al. One ordinary skill in the art would have been motivated to do so because deletion is a routine technique and a functional equivalent as insertion is as taught by Qi et al and admitted by the applicant, and Qi et al teach and demonstrate such routine technique in detail. The expectation of success would have been high, as deletion mutation is routine, taught and demonstrated in maize gene editing and knockout, for example, by Qi et al.
Therefore, the invention would have been obvious to one ordinary skill in the art.
Claims 85-86 and 24 are rejected under 35 U.S.C. 103 as being unpatentable over Gao et al in view of Kim et al and Qi et al, as applied to claims 1 and 22, and further in view of Duvick et al (US Patent 6627797, granted and published 9/30/2003), and Acevedo et al (USPGPUB 2003166855, published 9/4/2003).
The teachings of Gao et al in view of Kim et al and Qi et al have been analyzed above.
Claim 85 limits claim 1, wherein the at least one mutation is a deletion of about 1000 base pairs to about 5000 base pairs.
Claim 86 limits claim 1, wherein the at least one mutation is a deletion that is located at about 2200 or about 2300 base pairs from the 5' end.
Claim 24 limits claim 22, wherein the target site is within a region of the LOX gene, the region comprising a sequence having at least 90% sequence identity to a sequence comprising: (c) about nucleotide 2000 to about nucleotide 6510 of the nucleotide sequence of LOX3.
Gao et al teach knocking out maize LOX genes, but Gao et al in view of Kim et al and Qi et al do not explicitly teach the particular limitations.
According to the specification (p7, last para), SEQ ID NO: 79 is maize LOX3 coding sequence. By sequence listing, SEQ ID NO: 79 has 2595 base pairs.
Kim et al teach (disclose and characterize) SEQ ID NO: 80 as maize LOX3 protein sequence as analyzed above.
Duvick et al teach (disclose and characterize) a sequence 99.9% identical to SEQ ID NO: 79 as maize LOX3 coding sequence. See “Sequence Matches” at the end of office action.
Thus, deleting a deletion of about 5000 base pairs would encompass deleting entire coding sequence of the LOX3, the limitation of claim 85.
Deleting at about 2200 or about 2300 base pairs from the 5' end would encompass deleting significant portion(s) of coding sequence of the LOX3, the limitation of claim 86.
About nucleotide 2000 to about nucleotide 6510 (about 4510 nt) of the LOX3 gene would encompass deleting entire coding sequence of the LOX3, the limitation of claim 24.
Acevedo et al teach that a maize LOX sequence having about 1000 to about 3080 base pairs may still have LOX activity ([0043]), and suggest that deletion, substitution, truncation and insertion of LOX sequences will change LOX activities ([0047]).
Thus, it would have been obvious for one ordinary skill in the art to modify the invention of Gao et al, such that the knockout of LOX as taught by Gao et al is deleting an entire or significant portion of a LOX coding sequence, as taught and motivated by Duvick et al and Acevedo et al collectively. One ordinary skill in the art would have been motivated to do so because LOX3 coding sequence is 2595 nt long and had been disclosed and characterized, deleting entire or significant portion of a LOX encoding sequence would knockout the LOX, and one ordinary skill in the art would have expected a success of knockout by deleting entire or significant portion of a LOX encoding sequence.
Therefore, the dependent claims would have been obvious to one ordinary skill in the art.
Remarks
According to the specification (page 7) and sequence listing, SEQ ID NOs: 94, 96-106 are synthetic sequences (comprising deletions in specific positions) made by the applicant. By sequence search and basting, no prior art teaches any sequence 100% identical to any of SEQ ID NOs: 94, 96-106.
Hence, claims 15 and 62 are not rejected against prior art.
For compact prosecution, not only SEQ ID NO: 80 as analyzed above, but also SEQ ID NOs: 74, 77 and 83, and the coding sequences, had been searched to be taught by prior art. See “Sequence Matches” below.
Sequence Matches
Against SEQ ID NO: 80
RESULT 1
Q8W0V2_MAIZE
ID Q8W0V2_MAIZE Unreviewed; 864 AA.
AC Q8W0V2;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 28-JAN-2026, entry version 146.
DE RecName: Full=linoleate 9S-lipoxygenase {ECO:0000256|ARBA:ARBA00039006};
DE EC=1.13.11.58 {ECO:0000256|ARBA:ARBA00039006};
GN Name=lox3 {ECO:0000313|EnsemblPlants:Zm00001eb054040_P001};
GN ORFNames=ZEAMMB73_Zm00001d033623 {ECO:0000313|EMBL:ONM08085.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:AAL73499.1};
RN [1] {ECO:0000313|EMBL:AAL73499.1}
RP NUCLEOTIDE SEQUENCE.
RA Kim E.-S., Han O.S.;
RT "Genomic DNA of lipoxygenase gene.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ONM08085.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM08085.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb054040_P001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb054040_P001};
RA Seetharam A., Woodhouse M., Cannon E.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblPlants:Zm00001eb054040_P001}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb054040_P001};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding. Catalyzes the
CC hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene
CC structure. {ECO:0000256|ARBA:ARBA00056406}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC Evidence={ECO:0000256|ARBA:ARBA00036508};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962,
CC ECO:0000256|RuleBase:RU003974};
CC -!- SIMILARITY: Belongs to the lipoxygenase family.
CC {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR EMBL; AF465643; AAL73499.1; -; Genomic_DNA.
DR EMBL; CM007647; ONM08085.1; -; Genomic_DNA.
DR RefSeq; NP_001105515.1; NM_001112045.1.
DR AlphaFoldDB; Q8W0V2; -.
DR SMR; Q8W0V2; -.
DR PaxDb; 4577-GRMZM2G109130_P01; -.
DR EnsemblPlants; Zm00001eb054040_T001; Zm00001eb054040_P001; Zm00001eb054040.
DR GeneID; 542495; -.
DR Gramene; Zm00001eb054040_T001; Zm00001eb054040_P001; Zm00001eb054040.
DR KEGG; zma:542495; -.
DR eggNOG; ENOG502QQSP; Eukaryota.
DR OrthoDB; 407298at2759; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q8W0V2; baseline and differential.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051707; P:response to other organism; IEA:UniProtKB-ARBA.
DR GO; GO:0009611; P:response to wounding; IEA:UniProtKB-ARBA.
DR CDD; cd01751; PLAT_LH2; 1.
DR FunFam; 1.20.245.10:FF:000002; Lipoxygenase; 1.
DR FunFam; 2.60.60.20:FF:000015; Lipoxygenase; 1.
DR FunFam; 3.10.450.60:FF:000002; Lipoxygenase; 1.
DR FunFam; 4.10.372.10:FF:000001; Lipoxygenase; 1.
DR FunFam; 4.10.375.10:FF:000001; Lipoxygenase; 1.
DR Gene3D; 3.10.450.60; -; 1.
DR Gene3D; 4.10.375.10; Lipoxygenase-1, Domain 2; 1.
DR Gene3D; 4.10.372.10; Lipoxygenase-1, Domain 3; 1.
DR Gene3D; 1.20.245.10; Lipoxygenase-1, Domain 5; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003974};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003974};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767};
KW Proteomics identification {ECO:0007829|PeptideAtlas:Q8W0V2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT DOMAIN 39..159
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 162..864
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 208..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..237
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 864 AA; 96490 MW; 2E27D4E03A979FB5 CRC64;
Query Match 100.0%; Score 4561; Length 864;
Best Local Similarity 100.0%;
Matches 864; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MLSGIIDGLTGANKHARLKGTVVLMRKNVLDLNDFGATVVDSISEFLGKGVTCQLISSTL 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MLSGIIDGLTGANKHARLKGTVVLMRKNVLDLNDFGATVVDSISEFLGKGVTCQLISSTL 60
Qy 61 VDANNGNRGRVGAEANLEQWLTSLPSLTTGESKFGVTFDWEVEKLGVPGAVVVKNNHAAE 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 VDANNGNRGRVGAEANLEQWLTSLPSLTTGESKFGVTFDWEVEKLGVPGAVVVKNNHAAE 120
Qy 121 FFLKTITLDDVPGRGAVTFVANSWVYPAGKYRYNRVFFSNDTYLPSQMPAALKPYRDDEL 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 FFLKTITLDDVPGRGAVTFVANSWVYPAGKYRYNRVFFSNDTYLPSQMPAALKPYRDDEL 180
Qy 181 RNLRGDDQQGPYQEHDRVYRYDVYNDLGEPDGGNPRPILGGSADHPYPRRCRTGRKPTKT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 RNLRGDDQQGPYQEHDRVYRYDVYNDLGEPDGGNPRPILGGSADHPYPRRCRTGRKPTKT 240
Qy 241 DPNSESRLSLVEQIYVPRDERFGHLKMSDFLGYSIKAITQGIIPAVRTYVDTTPGEFDSF 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 DPNSESRLSLVEQIYVPRDERFGHLKMSDFLGYSIKAITQGIIPAVRTYVDTTPGEFDSF 300
Qy 301 QDIINLYEGGIKLPKIQALEDMRKLFPLQLVKDLLPAGGDYLLKLPIPQIIQEDKNAWRT 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 QDIINLYEGGIKLPKIQALEDMRKLFPLQLVKDLLPAGGDYLLKLPIPQIIQEDKNAWRT 360
Qy 361 DEEFAREVLAGVNPMVITRLTEFPPKSTLDPSKYGDHTSTITAEHIEKNLEGLTVQQALD 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 DEEFAREVLAGVNPMVITRLTEFPPKSTLDPSKYGDHTSTITAEHIEKNLEGLTVQQALD 420
Qy 421 GNRLYILDHHDRFMPFLIDVNNLEGNFIYATRTLFFLRGDGRLAPLAIELSEPYIDGDLT 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 GNRLYILDHHDRFMPFLIDVNNLEGNFIYATRTLFFLRGDGRLAPLAIELSEPYIDGDLT 480
Qy 481 VAKSKVYTPASSGVEAWVWQLAKAYVAVNDSGWHQLVSHWLNTHAVMEPFVIATNRQLSV 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 VAKSKVYTPASSGVEAWVWQLAKAYVAVNDSGWHQLVSHWLNTHAVMEPFVIATNRQLSV 540
Qy 541 THPVHKLLSSHFRDTMTINALARQTLINGGGIFEMTVFPGKYALGMSSVVYKSWNFTEQG 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 THPVHKLLSSHFRDTMTINALARQTLINGGGIFEMTVFPGKYALGMSSVVYKSWNFTEQG 600
Qy 601 LPADLVKRGVAVADPSSPYKVRLLIEDYPYASDGLAIWHAIEQWVGEYLAIYYPDDGALR 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 LPADLVKRGVAVADPSSPYKVRLLIEDYPYASDGLAIWHAIEQWVGEYLAIYYPDDGALR 660
Qy 661 GDEELQAWWKEVREVGHGDHKDAPWWPKMQAVSELASACTTIIWIASALHAAVNFGQYPY 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 GDEELQAWWKEVREVGHGDHKDAPWWPKMQAVSELASACTTIIWIASALHAAVNFGQYPY 720
Qy 721 AGYLPNRPTVSRRRMPEPGSKEYEELERDPERGFIHTITSQIQTIIGISLIEILSKHSSD 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 AGYLPNRPTVSRRRMPEPGSKEYEELERDPERGFIHTITSQIQTIIGISLIEILSKHSSD 780
Qy 781 EVYLGQRDTPEWTSDARALAAFKRFSDALVKIEGKVVGENRDPQLRNRNGPAEFPYMLLY 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 EVYLGQRDTPEWTSDARALAAFKRFSDALVKIEGKVVGENRDPQLRNRNGPAEFPYMLLY 840
Qy 841 PNTSDHSGAAAGLTAKGIPNSISI 864
||||||||||||||||||||||||
Db 841 PNTSDHSGAAAGLTAKGIPNSISI 864
Against SEQ ID NO: 79
RESULT 2
AAD64729
ID AAD64729 standard; DNA; 2595 BP.
XX
AC AAD64729;
XX
DT 11-JUN-2007 (revised)
DT 11-MAR-2004 (first entry)
XX
DE Maize lipoxygenase (CSSAP92) coding region DNA.
XX
KW Maize; lipoxygenase; CSSAP92; aflatoxin; gene therapy; plant protectant;
KW gene; ds.
XX
OS Zea mays.
XX
FH Key Location/Qualifiers
FT CDS 1..2595
FT /*tag= a
FT /product= "Maize lipoxygenase"
XX
CC PN US6627797-B1.
XX
CC PD 30-SEP-2003.
XX
CC PF 16-MAR-2001; 2001US-00810268.
XX
PR 21-MAR-2000; 2000US-0190950P.
XX
CC PA (TEXA ) UNIV TEXAS A & M SYSTEM.
CC PA (PION-) PIONEER HI-BRED INT INC.
XX
CC PI Duvick J, Maddox JR, Keller NP;
XX
DR WPI; 2003-874315/81.
DR P-PSDB; ABW02705.
DR PC:NCBI; gi12620876.
DR PC_ENCPRO:NCBI; gi12620877.
XX
CC PT New maize lipoxygenase polynucleotide, designated CSSAP92, useful for
CC PT altering lipoxygenase concentration in plants, for decreasing
CC PT accumulation of aflatoxin in plants, or for increasing the resistance of
CC PT plants to pathogens.
XX
CC PS Claim 1; SEQ ID NO 2; 0pp; English.
XX
CC The invention relates to maize lipoxygenase polynucleotide, designated
CC CSSAP92. The nucleic acid molecule and methods are useful in altering
CC lipoxygenase concentration in plants, in decreasing accumulation of
CC aflatoxin in plants, or in increasing the resistance of plants to
CC pathogens. The invention is useful in gene therapy. The present sequence
CC is maize lipoxygenase DNA
CC
CC Revised record issued on 11-JUN-2007 : Enhanced with precomputed
CC information from BOND.
XX
SQ Sequence 2595 BP; 505 A; 928 C; 802 G; 360 T; 0 U; 0 Other;
Query Match 99.9%; Score 2593.4; Length 2595;
Best Local Similarity 99.9%;
Matches 2594; Conservative 0; Mismatches 1; Indels 0; Gaps 0;
Qy 1 ATGCTGAGCGGGATCATCGACGGGCTGACGGGGGCGAACAAGCATGCGCGGCTCAAGGGC 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 ATGCTGAGCGGGATCATCGACGGGCTGACGGGGGCGAACAAGCATGCGCGGCTCAAGGGC 60
Qy 61 ACGGTGGTGCTCATGCGCAAGAACGTGCTGGACCTCAACGACTTCGGCGCCACCGTCGTT 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 ACGGTGGTGCTCATGCGCAAGAACGTGCTGGACCTCAACGACTTCGGCGCCACCGTCGTT 120
Qy 121 GACAGCATCAGCGAGTTCCTCGGCAAGGGGGTCACCTGCCAGCTCATCAGCTCCACCCTC 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 GACAGCATCAGCGAGTTCCTCGGCAAGGGGGTCACCTGCCAGCTCATCAGCTCCACCCTC 180
Qy 181 GTCGACGCCAACAACGGCAACCGCGGGCGGGTCGGGGCGGAGGCGAACCTGGAGCAGTGG 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 GTCGACGCCAACAACGGCAACCGCGGGCGGGTCGGGGCGGAGGCGAACCTGGAGCAGTGG 240
Qy 241 CTGACGAGCCTGCCGTCGCTGACGACCGGCGAGTCCAAGTTCGGCGTCACGTTCGACTGG 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 CTGACGAGCCTGCCGTCGCTGACGACCGGCGAGTCCAAGTTCGGCGTCACGTTCGACTGG 300
Qy 301 GAGGTGGAGAAGCTGGGAGTGCCGGGGGCCGTCGTCGTCAAGAACAACCACGCCGCCGAG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 GAGGTGGAGAAGCTGGGAGTGCCGGGGGCCGTCGTCGTCAAGAACAACCACGCCGCCGAG 360
Qy 361 TTCTTCCTCAAGACAATCACCCTCGACGACGTGCCCGGCCGCGGCGCCGTCACCTTCGTC 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 TTCTTCCTCAAGACAATCACCCTCGACGACGTGCCCGGCCGCGGCGCCGTCACCTTCGTC 420
Qy 421 GCCAACTCCTGGGTCTACCCCGCGGGCAAGTACCGCTACAACCGCGTCTTCTTCTCCAAC 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 GCCAACTCCTGGGTCTACCCCGCGGGCAAGTACCGCTACAACCGCGTCTTCTTCTCCAAC 480
Qy 481 GATACGTACCTGCCAAGCCAGATGCCGGCGGCGCTGAAGCCGTACCGCGACGACGAGCTC 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 GATACGTACCTGCCAAGCCAGATGCCGGCGGCGCTGAAGCCGTACCGCGACGACGAGCTC 540
Qy 541 CGCAACCTCCGCGGCGACGACCAGCAGGGCCCCTACCAGGAGCACGACCGCGTGTACCGC 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 CGCAACCTCCGCGGCGACGACCAGCAGGGCCCCTACCAGGAGCACGACCGCGTGTACCGC 600
Qy 601 TACGACGTCTACAACGACCTCGGCGAGCCCGACGGCGGCAACCCGCGCCCCATCCTCGGC 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 TACGACGTCTACAACGACCTCGGCGAGCCCGACGGCGGCAACCCGCGCCCCATCCTCGGC 660
Qy 661 GGCTCCGCCGACCACCCGTACCCGCGCCGCTGCCGCACGGGCCGCAAGCCCACCAAAACC 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 GGCTCCGCCGACCACCCGTACCCGCGCCGCTGCCGCACGGGCCGCAAGCCCACCAAAACC 720
Qy 721 GACCCCAACTCGGAGAGCCGACTGTCGCTGGTGGAGCAGATCTACGTGCCGCGGGACGAG 780
|||||||||||||| |||||||||||||||||||||||||||||||||||||||||||||
Db 721 GACCCCAACTCGGATAGCCGACTGTCGCTGGTGGAGCAGATCTACGTGCCGCGGGACGAG 780
Qy 781 CGCTTCGGCCACCTCAAGATGTCCGACTTCCTGGGCTACTCCATCAAGGCCATCACGCAG 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 CGCTTCGGCCACCTCAAGATGTCCGACTTCCTGGGCTACTCCATCAAGGCCATCACGCAG 840
Qy 841 GGCATCATCCCGGCGGTGCGCACGTACGTGGACACCACCCCGGGCGAGTTCGACTCCTTC 900
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 GGCATCATCCCGGCGGTGCGCACGTACGTGGACACCACCCCGGGCGAGTTCGACTCCTTC 900
Qy 901 CAGGACATCATCAACCTGTACGAGGGCGGGATCAAGCTGCCCAAGATCCAGGCGCTCGAG 960
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 901 CAGGACATCATCAACCTGTACGAGGGCGGGATCAAGCTGCCCAAGATCCAGGCGCTCGAG 960
Qy 961 GACATGCGCAAGCTCTTCCCGCTCCAGCTCGTCAAGGACCTCCTCCCCGCCGGCGGGGAC 1020
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 961 GACATGCGCAAGCTCTTCCCGCTCCAGCTCGTCAAGGACCTCCTCCCCGCCGGCGGGGAC 1020
Qy 1021 TACCTGCTCAAGCTCCCCATCCCACAGATCATCCAAGAGGACAAGAACGCGTGGAGGACC 1080
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1021 TACCTGCTCAAGCTCCCCATCCCACAGATCATCCAAGAGGACAAGAACGCGTGGAGGACC 1080
Qy 1081 GACGAGGAGTTCGCGCGGGAGGTGCTCGCCGGCGTCAACCCGATGGTGATCACGCGCCTC 1140
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1081 GACGAGGAGTTCGCGCGGGAGGTGCTCGCCGGCGTCAACCCGATGGTGATCACGCGCCTC 1140
Qy 1141 ACGGAGTTCCCGCCCAAGAGCACGCTGGACCCCAGCAAGTACGGCGACCACACCAGCACG 1200
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1141 ACGGAGTTCCCGCCCAAGAGCACGCTGGACCCCAGCAAGTACGGCGACCACACCAGCACG 1200
Qy 1201 ATCACGGCGGAGCACATCGAGAAGAACCTCGAGGGCCTCACGGTGCAGCAGGCGCTGGAC 1260
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1201 ATCACGGCGGAGCACATCGAGAAGAACCTCGAGGGCCTCACGGTGCAGCAGGCGCTGGAC 1260
Qy 1261 GGCAACAGGCTCTACATCCTGGACCACCACGACCGCTTCATGCCGTTCCTCATCGACGTC 1320
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1261 GGCAACAGGCTCTACATCCTGGACCACCACGACCGCTTCATGCCGTTCCTCATCGACGTC 1320
Qy 1321 AACAACCTGGAGGGCAACTTCATCTACGCCACCAGGACGCTCTTCTTCCTGCGCGGCGAC 1380
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1321 AACAACCTGGAGGGCAACTTCATCTACGCCACCAGGACGCTCTTCTTCCTGCGCGGCGAC 1380
Qy 1381 GGCAGGCTCGCGCCCCTCGCCATCGAGCTCAGCGAGCCGTACATCGACGGGGACCTCACC 1440
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1381 GGCAGGCTCGCGCCCCTCGCCATCGAGCTCAGCGAGCCGTACATCGACGGGGACCTCACC 1440
Qy 1441 GTGGCCAAGAGCAAGGTCTACACGCCGGCGTCCAGCGGCGTCGAGGCCTGGGTGTGGCAG 1500
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1441 GTGGCCAAGAGCAAGGTCTACACGCCGGCGTCCAGCGGCGTCGAGGCCTGGGTGTGGCAG 1500
Qy 1501 CTCGCCAAGGCCTATGTCGCCGTCAACGACTCTGGCTGGCACCAACTCGTCAGCCACTGG 1560
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1501 CTCGCCAAGGCCTATGTCGCCGTCAACGACTCTGGCTGGCACCAACTCGTCAGCCACTGG 1560
Qy 1561 CTGAACACCCACGCGGTGATGGAGCCGTTCGTGATCGCGACGAACCGGCAGCTGAGCGTG 1620
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1561 CTGAACACCCACGCGGTGATGGAGCCGTTCGTGATCGCGACGAACCGGCAGCTGAGCGTG 1620
Qy 1621 ACGCACCCGGTGCACAAGCTCCTGAGCTCGCACTTCCGCGACACCATGACCATCAACGCG 1680
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1621 ACGCACCCGGTGCACAAGCTCCTGAGCTCGCACTTCCGCGACACCATGACCATCAACGCG 1680
Qy 1681 CTGGCGCGGCAGACGCTCATCAACGGCGGCGGCATCTTCGAGATGACCGTCTTCCCGGGC 1740
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1681 CTGGCGCGGCAGACGCTCATCAACGGCGGCGGCATCTTCGAGATGACCGTCTTCCCGGGC 1740
Qy 1741 AAGTACGCGCTGGGCATGTCCTCCGTGGTGTACAAGAGCTGGAACTTCACCGAGCAGGGC 1800
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1741 AAGTACGCGCTGGGCATGTCCTCCGTGGTGTACAAGAGCTGGAACTTCACCGAGCAGGGC 1800
Qy 1801 CTCCCCGCCGACCTCGTCAAGAGGGGCGTGGCGGTGGCGGACCCGTCCAGCCCGTACAAG 1860
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1801 CTCCCCGCCGACCTCGTCAAGAGGGGCGTGGCGGTGGCGGACCCGTCCAGCCCGTACAAG 1860
Qy 1861 GTGCGGCTGCTGATCGAGGACTACCCGTACGCGAGCGACGGGCTGGCCATCTGGCACGCC 1920
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1861 GTGCGGCTGCTGATCGAGGACTACCCGTACGCGAGCGACGGGCTGGCCATCTGGCACGCC 1920
Qy 1921 ATCGAGCAGTGGGTGGGCGAGTACCTGGCCATCTACTACCCCGACGACGGCGCGCTGCGG 1980
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1921 ATCGAGCAGTGGGTGGGCGAGTACCTGGCCATCTACTACCCCGACGACGGCGCGCTGCGG 1980
Qy 1981 GGCGACGAGGAGCTGCAGGCGTGGTGGAAGGAGGTGCGCGAGGTCGGGCACGGCGACCAC 2040
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1981 GGCGACGAGGAGCTGCAGGCGTGGTGGAAGGAGGTGCGCGAGGTCGGGCACGGCGACCAC 2040
Qy 2041 AAGGACGCGCCCTGGTGGCCCAAGATGCAGGCCGTGTCGGAGCTCGCCAGCGCCTGCACC 2100
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2041 AAGGACGCGCCCTGGTGGCCCAAGATGCAGGCCGTGTCGGAGCTCGCCAGCGCCTGCACC 2100
Qy 2101 ACCATCATCTGGATCGCGTCGGCGCTCCACGCCGCCGTCAACTTCGGCCAGTACCCGTAC 2160
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2101 ACCATCATCTGGATCGCGTCGGCGCTCCACGCCGCCGTCAACTTCGGCCAGTACCCGTAC 2160
Qy 2161 GCGGGGTACCTCCCGAACAGGCCCACGGTGAGCCGGCGCCGGATGCCGGAGCCCGGCAGC 2220
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2161 GCGGGGTACCTCCCGAACAGGCCCACGGTGAGCCGGCGCCGGATGCCGGAGCCCGGCAGC 2220
Qy 2221 AAGGAGTACGAGGAGCTGGAGCGCGACCCGGAGCGCGGCTTCATCCACACCATCACGAGC 2280
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2221 AAGGAGTACGAGGAGCTGGAGCGCGACCCGGAGCGCGGCTTCATCCACACCATCACGAGC 2280
Qy 2281 CAGATCCAGACCATCATCGGCATCTCGCTCATCGAGATCCTCTCCAAGCACTCCTCCGAC 2340
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2281 CAGATCCAGACCATCATCGGCATCTCGCTCATCGAGATCCTCTCCAAGCACTCCTCCGAC 2340
Qy 2341 GAGGTGTACCTCGGCCAGCGCGACACCCCCGAGTGGACCTCCGACGCCCGGGCGCTGGCG 2400
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2341 GAGGTGTACCTCGGCCAGCGCGACACCCCCGAGTGGACCTCCGACGCCCGGGCGCTGGCG 2400
Qy 2401 GCGTTCAAGAGGTTCAGCGACGCGCTGGTCAAGATCGAGGGCAAGGTGGTGGGCGAGAAC 2460
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2401 GCGTTCAAGAGGTTCAGCGACGCGCTGGTCAAGATCGAGGGCAAGGTGGTGGGCGAGAAC 2460
Qy 2461 CGCGACCCGCAGCTGAGGAACAGGAACGGCCCCGCCGAGTTCCCCTACATGCTGCTCTAT 2520
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2461 CGCGACCCGCAGCTGAGGAACAGGAACGGCCCCGCCGAGTTCCCCTACATGCTGCTCTAT 2520
Qy 2521 CCCAACACCTCTGACCACAGTGGCGCCGCCGCAGGGCTCACTGCCAAGGGCATCCCCAAC 2580
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2521 CCCAACACCTCTGACCACAGTGGCGCCGCCGCAGGGCTCACTGCCAAGGGCATCCCCAAC 2580
Qy 2581 AGCATCTCCATCTGA 2595
|||||||||||||||
Db 2581 AGCATCTCCATCTGA 2595
Against SEQ ID NO: 74
RESULT 1
A0A1D6N531_MAIZE
ID A0A1D6N531_MAIZE Unreviewed; 884 AA.
AC A0A1D6N531;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 28-JAN-2026, entry version 43.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN ORFNames=ZEAMMB73_Zm00001d042541 {ECO:0000313|EMBL:ONM35737.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM35737.1};
RN [1] {ECO:0000313|EMBL:ONM35737.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM35737.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding.
CC {ECO:0000256|RuleBase:RU003975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC Evidence={ECO:0000256|ARBA:ARBA00036508};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962,
CC ECO:0000256|RuleBase:RU003974};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000256|RuleBase:RU003975}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family.
CC {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
CC ---------------------------------------------------------------------------
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DR EMBL; CM007649; ONM35737.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D6N531; -.
DR SMR; A0A1D6N531; -.
DR IntAct; A0A1D6N531; 1.
DR STRING; 4577.A0A1D6N531; -.
DR InParanoid; A0A1D6N531; -.
DR UniPathway; UPA00382; -.
DR ExpressionAtlas; A0A1D6N531; baseline and differential.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IEA:InterPro.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0051707; P:response to other organism; IEA:UniProtKB-ARBA.
DR GO; GO:0009611; P:response to wounding; IEA:UniProtKB-ARBA.
DR CDD; cd01751; PLAT_LH2; 1.
DR FunFam; 1.20.245.10:FF:000002; Lipoxygenase; 1.
DR FunFam; 3.10.450.60:FF:000002; Lipoxygenase; 1.
DR FunFam; 4.10.372.10:FF:000001; Lipoxygenase; 1.
DR FunFam; 4.10.375.10:FF:000001; Lipoxygenase; 1.
DR Gene3D; 3.10.450.60; -; 1.
DR Gene3D; 4.10.375.10; Lipoxygenase-1, Domain 2; 1.
DR Gene3D; 4.10.372.10; Lipoxygenase-1, Domain 3; 1.
DR Gene3D; 1.20.245.10; Lipoxygenase-1, Domain 5; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU003975};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU003975};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003974};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003974};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW ECO:0000256|RuleBase:RU003975}.
FT REGION 229..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 99329 MW; 8F0F468628E4A592 CRC64;
Query Match 100.0%; Score 4672; Length 884;
Best Local Similarity 100.0%;
Matches 884; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MFGNIGKIPIIGDLTGSNKNAHLKGNVVLVRKTVLGLDVTSIAGSLLDGIGEFLGRGVTC 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MFGNIGKIPIIGDLTGSNKNAHLKGNVVLVRKTVLGLDVTSIAGSLLDGIGEFLGRGVTC 60
Qy 61 QLISSTVVDPTTLTGARVHRADNGNRGKLGAEASLEQWLLNPPPLLSSENQFRVTFDWEV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 QLISSTVVDPTTLTGARVHRADNGNRGKLGAEASLEQWLLNPPPLLSSENQFRVTFDWEV 120
Qy 121 EKQGIPGAIIVKNNHASEFFLKTITLNDVPGHGTIVFVANSWIYPQSKYRYNRVFFSNDT 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 EKQGIPGAIIVKNNHASEFFLKTITLNDVPGHGTIVFVANSWIYPQSKYRYNRVFFSNDT 180
Qy 181 YLPSQMPAALKPYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGLPDSGNPRPVLGGT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 YLPSQMPAALKPYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGLPDSGNPRPVLGGT 240
Qy 241 KELPYPRRCRTGRKPTKSDPNSESRLTLVDGDVYVPRDERFGHIKKSDFYGYAIKALVNA 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 KELPYPRRCRTGRKPTKSDPNSESRLTLVDGDVYVPRDERFGHIKKSDFYGYAIKALVNA 300
Qy 301 VIPAIRTYVDLSPGEFDSFKDIMKLYEGGIQLPKIPALEDLRKQFPLELVKDVLPVGGDY 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 VIPAIRTYVDLSPGEFDSFKDIMKLYEGGIQLPKIPALEDLRKQFPLELVKDVLPVGGDY 360
Qy 361 LLKLPMPQIIKEDKTGWMTDEEFGREILAGVNPMLVKRLTEFPPRSSLDPSKYGDHTSTI 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 LLKLPMPQIIKEDKTGWMTDEEFGREILAGVNPMLVKRLTEFPPRSSLDPSKYGDHTSTI 420
Qy 421 READLENKLEGLTVQQALHGNRLYILDHHDNFMPFLVRVNSLEGNFIYATRTVLFLRGDG 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 READLENKLEGLTVQQALHGNRLYILDHHDNFMPFLVRVNSLEGNFIYATRTVLFLRGDG 480
Qy 481 TLVPVAIELSLPELRDGLTTAKSTVYTPKSTTGAEAWVWHLAKAYANVNDYCWHQLISHW 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 TLVPVAIELSLPELRDGLTTAKSTVYTPKSTTGAEAWVWHLAKAYANVNDYCWHQLISHW 540
Qy 541 LNTHAVMEPFVIATNRQLSVTHPVHKLLLPHYRDTMNINSNARQMLVNAGGIFETTVFPR 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 LNTHAVMEPFVIATNRQLSVTHPVHKLLLPHYRDTMNINSNARQMLVNAGGIFETTVFPR 600
Qy 601 QYAFEMSSVIYKDWNFTEQALPDDLIKRGMAVADPSSPYKVRLLVEDYPYASDGLAIWHA 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 QYAFEMSSVIYKDWNFTEQALPDDLIKRGMAVADPSSPYKVRLLVEDYPYASDGLAIWHA 660
Qy 661 IEQWVTEYLAVYYPNDGVLRADVELQAWWKEAREVGHADLKDAPWWPKMQTVAELVKACT 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 IEQWVTEYLAVYYPNDGVLRADVELQAWWKEAREVGHADLKDAPWWPKMQTVAELVKACT 720
Qy 721 TIIWIASALHAAVNFGQYPYAGYLPNRPSVSRKPMPAPGSDEYAELERKPEKVFVRTITS 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 TIIWIASALHAAVNFGQYPYAGYLPNRPSVSRKPMPAPGSDEYAELERKPEKVFVRTITS 780
Qy 781 QFQALVGISLLEILSSHSSDEVYLGQRDTKEWTSDAKAQEAFKRFGARLTEIEKRVVTMN 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 QFQALVGISLLEILSSHSSDEVYLGQRDTKEWTSDAKAQEAFKRFGARLTEIEKRVVTMN 840
Qy 841 ADPRLKNRNGPAEFPYTLLYPNTSDTKGDAAGITAKGIPNSISI 884
||||||||||||||||||||||||||||||||||||||||||||
Db 841 ADPRLKNRNGPAEFPYTLLYPNTSDTKGDAAGITAKGIPNSISI 884
RESULT 2
US-10-132-350-2
(NOTE: this sequence has 15 duplicates in the database searched.
See complete list at the end of this report)
Sequence 2, US/10132350
Publication No. US20030166855A1
GENERAL INFORMATION
APPLICANT: Acevedo, Pedro A. Navarro
APPLICANT: Duvick, Jonathan P.
APPLICANT: Kolomiets, Mikhailo V.
APPLICANT: Simmons, Carl R.
TITLE OF INVENTION: Lipoxygenase Polynucleotides and Methods
TITLE OF INVENTION: of Use
FILE REFERENCE: 35718/246439
CURRENT APPLICATION NUMBER: US/10/132,350
CURRENT FILING DATE: 2002-04-25
PRIOR APPLICATION NUMBER: US 60/286,889
PRIOR FILING DATE: 2001-04-27
PRIOR APPLICATION NUMBER: US 60/305,366
PRIOR FILING DATE: 2001-07-13
NUMBER OF SEQ ID NOS: 56
SEQ ID NO 2
LENGTH: 873
TYPE: PRT
ORGANISM: Zea mays
Query Match 98.4%; Score 4596.5; Length 873;
Best Local Similarity 98.6%;
Matches 872; Conservative 1; Mismatches 0; Indels 11; Gaps 1;
Qy 1 MFGNIGKIPIIGDLTGSNKNAHLKGNVVLVRKTVLGLDVTSIAGSLLDGIGEFLGRGVTC 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MFGNIGKIPIIGDLTGSNKNAHLKGNVVLVRKTVLGLDVTSIAGSLLDGIGEFLGRGVTC 60
Qy 61 QLISSTVVDPTTLTGARVHRADNGNRGKLGAEASLEQWLLNPPPLLSSENQFRVTFDWEV 120
|||||||||| :||||||||||||||||||||||||||||||||||||||
Db 61 QLISSTVVDP-----------NNGNRGKLGAEASLEQWLLNPPPLLSSENQFRVTFDWEV 109
Qy 121 EKQGIPGAIIVKNNHASEFFLKTITLNDVPGHGTIVFVANSWIYPQSKYRYNRVFFSNDT 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 110 EKQGIPGAIIVKNNHASEFFLKTITLNDVPGHGTIVFVANSWIYPQSKYRYNRVFFSNDT 169
Qy 181 YLPSQMPAALKPYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGLPDSGNPRPVLGGT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 170 YLPSQMPAALKPYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGLPDSGNPRPVLGGT 229
Qy 241 KELPYPRRCRTGRKPTKSDPNSESRLTLVDGDVYVPRDERFGHIKKSDFYGYAIKALVNA 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 230 KELPYPRRCRTGRKPTKSDPNSESRLTLVDGDVYVPRDERFGHIKKSDFYGYAIKALVNA 289
Qy 301 VIPAIRTYVDLSPGEFDSFKDIMKLYEGGIQLPKIPALEDLRKQFPLELVKDVLPVGGDY 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 290 VIPAIRTYVDLSPGEFDSFKDIMKLYEGGIQLPKIPALEDLRKQFPLELVKDVLPVGGDY 349
Qy 361 LLKLPMPQIIKEDKTGWMTDEEFGREILAGVNPMLVKRLTEFPPRSSLDPSKYGDHTSTI 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 350 LLKLPMPQIIKEDKTGWMTDEEFGREILAGVNPMLVKRLTEFPPRSSLDPSKYGDHTSTI 409
Qy 421 READLENKLEGLTVQQALHGNRLYILDHHDNFMPFLVRVNSLEGNFIYATRTVLFLRGDG 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 410 READLENKLEGLTVQQALHGNRLYILDHHDNFMPFLVRVNSLEGNFIYATRTVLFLRGDG 469
Qy 481 TLVPVAIELSLPELRDGLTTAKSTVYTPKSTTGAEAWVWHLAKAYANVNDYCWHQLISHW 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 470 TLVPVAIELSLPELRDGLTTAKSTVYTPKSTTGAEAWVWHLAKAYANVNDYCWHQLISHW 529
Qy 541 LNTHAVMEPFVIATNRQLSVTHPVHKLLLPHYRDTMNINSNARQMLVNAGGIFETTVFPR 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 530 LNTHAVMEPFVIATNRQLSVTHPVHKLLLPHYRDTMNINSNARQMLVNAGGIFETTVFPR 589
Qy 601 QYAFEMSSVIYKDWNFTEQALPDDLIKRGMAVADPSSPYKVRLLVEDYPYASDGLAIWHA 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 590 QYAFEMSSVIYKDWNFTEQALPDDLIKRGMAVADPSSPYKVRLLVEDYPYASDGLAIWHA 649
Qy 661 IEQWVTEYLAVYYPNDGVLRADVELQAWWKEAREVGHADLKDAPWWPKMQTVAELVKACT 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 650 IEQWVTEYLAVYYPNDGVLRADVELQAWWKEAREVGHADLKDAPWWPKMQTVAELVKACT 709
Qy 721 TIIWIASALHAAVNFGQYPYAGYLPNRPSVSRKPMPAPGSDEYAELERKPEKVFVRTITS 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 710 TIIWIASALHAAVNFGQYPYAGYLPNRPSVSRKPMPAPGSDEYAELERKPEKVFVRTITS 769
Qy 781 QFQALVGISLLEILSSHSSDEVYLGQRDTKEWTSDAKAQEAFKRFGARLTEIEKRVVTMN 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 770 QFQALVGISLLEILSSHSSDEVYLGQRDTKEWTSDAKAQEAFKRFGARLTEIEKRVVTMN 829
Qy 841 ADPRLKNRNGPAEFPYTLLYPNTSDTKGDAAGITAKGIPNSISI 884
||||||||||||||||||||||||||||||||||||||||||||
Db 830 ADPRLKNRNGPAEFPYTLLYPNTSDTKGDAAGITAKGIPNSISI 873
Against SEQ ID NO: 73
RESULT 2
ADG93372
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
ID ADG93372 standard; DNA; 2622 BP.
XX
AC ADG93372;
XX
DT 11-MAR-2004 (first entry)
XX
DE Maize lipoxygenase (LOX) DNA #2.
XX
KW Maize; lipoxygenase; LOX; corn; gene; ds; plant;
KW plant pathogen defence system; plant development; tissue healing;
KW mycotoxin; aflatoxin; sterigmatocystin.
XX
OS Zea mays.
XX
CC PN US2003166855-A1.
XX
CC PD 04-SEP-2003.
XX
CC PF 25-APR-2002; 2002US-00132350.
XX
PR 27-APR-2001; 2001US-0286889P.
PR 13-JUL-2001; 2001US-0305366P.
XX
CC PA (PION-) PIONEER HI-BRED INT INC.
XX
CC PI Navarro Acevedo PA, Duvick JP, Kolomiets MV, Simmons CR;
XX
DR WPI; 2003-898106/82.
DR P-PSDB; ADG93373.
XX
CC PT New lipoxygenase polypeptides and polynucleotides, useful for enhancing
CC PT resistance to pathogens, e.g. fungi, viruses, nematodes or insects, for
CC PT promoting healing of damage tissues, or for modulating plant growth and
CC PT development.
XX
CC PS Disclosure; SEQ ID NO 3; 151pp; English.
XX
CC The invention relates to maize lipoxygenase (LOX) polypeptides and
CC polynucleotides encoding the polypeptides. The LOX polypeptides and
CC polynucleotides are useful in modulating plant pathogen defence systems
CC (particularly enhancing resistance to fungi, viruses, nematodes and
CC insects) and plant development, and for promoting healing of damaged
CC tissues. LOX proteins may also be used to inhibit the production of
CC mycotoxins of fungi (e.g. aflatoxin) and sterigmatocystin producing
CC fungus in plants susceptible to contamination by the mycotoxins. This
CC sequence represents DNA encoding a maize LOX polypeptide of the
CC invention.
XX
SQ Sequence 2622 BP; 534 A; 934 C; 773 G; 381 T; 0 U; 0 Other;
Query Match 97.1%; Score 2579; Length 2622;
Best Local Similarity 98.8%;
Matches 2622; Conservative 0; Mismatches 0; Indels 33; Gaps 1;
Qy 1 ATGTTCGGGAACATCGGAAAGATCCCCATCATCGGCGACCTGACGGGCAGCAACAAGAAT 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 ATGTTCGGGAACATCGGAAAGATCCCCATCATCGGCGACCTGACGGGCAGCAACAAGAAT 60
Qy 61 GCGCACCTCAAGGGCAACGTGGTGCTCGTGCGCAAGACCGTGCTCGGCTTGGACGTCACC 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GCGCACCTCAAGGGCAACGTGGTGCTCGTGCGCAAGACCGTGCTCGGCTTGGACGTCACC 120
Qy 121 AGCATCGCCGGCTCCCTCCTCGACGGCATCGGCGAGTTCCTCGGCCGCGGCGTCACCTGC 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 AGCATCGCCGGCTCCCTCCTCGACGGCATCGGCGAGTTCCTCGGCCGCGGCGTCACCTGC 180
Qy 181 CAGCTTATCAGCTCCACCGTCGTCGACCCTACGACGCTGACCGGCGCGCGCGTGCACCGT 240
|||||||||||||||||||||||||||||||
Db 181 CAGCTTATCAGCTCCACCGTCGTCGACCCTA----------------------------- 211
Qy 241 GCAGACAACGGCAACCGCGGGAAGTTGGGCGCGGAGGCGAGCCTGGAGCAGTGGCTGCTG 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 212 ----ACAACGGCAACCGCGGGAAGTTGGGCGCGGAGGCGAGCCTGGAGCAGTGGCTGCTG 267
Qy 301 AACCCGCCGCCGCTTCTGTCCAGCGAGAACCAGTTCCGCGTCACCTTCGACTGGGAGGTG 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 268 AACCCGCCGCCGCTTCTGTCCAGCGAGAACCAGTTCCGCGTCACCTTCGACTGGGAGGTG 327
Qy 361 GAGAAGCAGGGCATCCCGGGCGCCATCATCGTCAAGAACAACCACGCCTCCGAGTTCTTC 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 328 GAGAAGCAGGGCATCCCGGGCGCCATCATCGTCAAGAACAACCACGCCTCCGAGTTCTTC 387
Qy 421 CTCAAGACCATCACCCTCAACGACGTCCCCGGCCACGGCACCATCGTCTTCGTCGCCAAC 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 388 CTCAAGACCATCACCCTCAACGACGTCCCCGGCCACGGCACCATCGTCTTCGTCGCCAAC 447
Qy 481 TCATGGATCTACCCGCAGTCCAAGTACCGCTACAACCGCGTCTTCTTCTCCAACGACACG 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 448 TCATGGATCTACCCGCAGTCCAAGTACCGCTACAACCGCGTCTTCTTCTCCAACGACACG 507
Qy 541 TACCTCCCCAGCCAGATGCCGGCGGCGCTGAAGCCCTACCGCGACGACGAGCTCCGGAAC 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 508 TACCTCCCCAGCCAGATGCCGGCGGCGCTGAAGCCCTACCGCGACGACGAGCTCCGGAAC 567
Qy 601 CTGAGGGGCGACGACCAGCAGGGCCCGTACCAGGAGCACGACCGCGTCTACCGCTACGAC 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 568 CTGAGGGGCGACGACCAGCAGGGCCCGTACCAGGAGCACGACCGCGTCTACCGCTACGAC 627
Qy 661 GTCTACAACGACCTGGGCCTGCCTGACAGCGGGAACCCGCGCCCCGTCCTCGGCGGCACC 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 628 GTCTACAACGACCTGGGCCTGCCTGACAGCGGGAACCCGCGCCCCGTCCTCGGCGGCACC 687
Qy 721 AAGGAGCTCCCCTACCCGCGCCGCTGCCGCACCGGGCGGAAGCCCACCAAGAGCGACCCC 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 688 AAGGAGCTCCCCTACCCGCGCCGCTGCCGCACCGGGCGGAAGCCCACCAAGAGCGACCCC 747
Qy 781 AACAGCGAGAGCAGGCTCACGCTGGTCGACGGCGACGTCTACGTGCCGCGCGACGAGCGC 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 748 AACAGCGAGAGCAGGCTCACGCTGGTCGACGGCGACGTCTACGTGCCGCGCGACGAGCGC 807
Qy 841 TTCGGCCACATCAAGAAGTCGGACTTCTACGGCTACGCCATCAAGGCGCTGGTGAACGCC 900
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 808 TTCGGCCACATCAAGAAGTCGGACTTCTACGGCTACGCCATCAAGGCGCTGGTGAACGCC 867
Qy 901 GTCATCCCGGCAATCCGCACCTACGTCGACCTGTCGCCCGGCGAGTTCGACTCCTTCAAG 960
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 868 GTCATCCCGGCAATCCGCACCTACGTCGACCTGTCGCCCGGCGAGTTCGACTCCTTCAAG 927
Qy 961 GACATCATGAAGCTGTACGAGGGCGGGATCCAGCTGCCCAAAATACCAGCCCTCGAGGAC 1020
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 928 GACATCATGAAGCTGTACGAGGGCGGGATCCAGCTGCCCAAAATACCAGCCCTCGAGGAC 987
Qy 1021 CTGCGGAAGCAGTTCCCACTCGAGCTCGTCAAGGATGTCCTCCCGGTCGGCGGCGACTAC 1080
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 988 CTGCGGAAGCAGTTCCCACTCGAGCTCGTCAAGGATGTCCTCCCGGTCGGCGGCGACTAC 1047
Qy 1081 CTCCTCAAGCTCCCCATGCCGCAGATCATCAAAGAGGACAAGACAGGTTGGATGACAGAT 1140
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1048 CTCCTCAAGCTCCCCATGCCGCAGATCATCAAAGAGGACAAGACAGGTTGGATGACAGAT 1107
Qy 1141 GAGGAGTTTGGACGGGAGATTCTCGCCGGCGTGAACCCCATGCTCGTCAAGCGTCTCACG 1200
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1108 GAGGAGTTTGGACGGGAGATTCTCGCCGGCGTGAACCCCATGCTCGTCAAGCGTCTCACG 1167
Qy 1201 GAGTTCCCTCCGAGGAGCAGTCTTGACCCGAGCAAGTACGGCGACCACACCAGCACCATC 1260
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1168 GAGTTCCCTCCGAGGAGCAGTCTTGACCCGAGCAAGTACGGCGACCACACCAGCACCATC 1227
Qy 1261 AGGGAGGCGGACCTCGAGAACAAGCTCGAGGGCCTGACGGTGCAGCAGGCGCTGCACGGC 1320
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1228 AGGGAGGCGGACCTCGAGAACAAGCTCGAGGGCCTGACGGTGCAGCAGGCGCTGCACGGC 1287
Qy 1321 AACCGGCTCTACATCCTGGACCACCACGACAACTTCATGCCGTTCCTGGTCAGGGTGAAC 1380
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1288 AACCGGCTCTACATCCTGGACCACCACGACAACTTCATGCCGTTCCTGGTCAGGGTGAAC 1347
Qy 1381 AGCCTGGAGGGCAACTTCATCTACGCCACCAGGACCGTGCTGTTCCTGCGCGGCGACGGC 1440
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1348 AGCCTGGAGGGCAACTTCATCTACGCCACCAGGACCGTGCTGTTCCTGCGCGGCGACGGC 1407
Qy 1441 ACGCTGGTGCCGGTGGCCATCGAGCTGAGCCTGCCCGAGCTCCGGGACGGCCTGACCACC 1500
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1408 ACGCTGGTGCCGGTGGCCATCGAGCTGAGCCTGCCCGAGCTCCGGGACGGCCTGACCACC 1467
Qy 1501 GCCAAGAGCACCGTGTACACGCCCAAGTCGACCACCGGCGCGGAGGCGTGGGTGTGGCAC 1560
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1468 GCCAAGAGCACCGTGTACACGCCCAAGTCGACCACCGGCGCGGAGGCGTGGGTGTGGCAC 1527
Qy 1561 CTGGCCAAGGCCTACGCCAACGTGAACGACTACTGCTGGCACCAGCTCATCAGCCACTGG 1620
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1528 CTGGCCAAGGCCTACGCCAACGTGAACGACTACTGCTGGCACCAGCTCATCAGCCACTGG 1587
Qy 1621 CTCAACACCCACGCCGTGATGGAGCCGTTCGTGATCGCCACCAACCGGCAGCTCAGCGTG 1680
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1588 CTCAACACCCACGCCGTGATGGAGCCGTTCGTGATCGCCACCAACCGGCAGCTCAGCGTG 1647
Qy 1681 ACGCACCCCGTGCACAAGCTCCTCCTGCCGCACTACCGTGACACCATGAACATCAACTCC 1740
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1648 ACGCACCCCGTGCACAAGCTCCTCCTGCCGCACTACCGTGACACCATGAACATCAACTCC 1707
Qy 1741 AACGCGCGCCAGATGCTCGTCAACGCCGGCGGCATCTTCGAGACCACCGTCTTCCCGCGC 1800
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1708 AACGCGCGCCAGATGCTCGTCAACGCCGGCGGCATCTTCGAGACCACCGTCTTCCCGCGC 1767
Qy 1801 CAGTACGCGTTCGAGATGTCCTCCGTCATCTACAAGGACTGGAACTTCACAGAGCAGGCT 1860
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1768 CAGTACGCGTTCGAGATGTCCTCCGTCATCTACAAGGACTGGAACTTCACAGAGCAGGCT 1827
Qy 1861 CTCCCTGACGACCTAATCAAGAGAGGCATGGCGGTCGCAGACCCGTCGAGCCCGTACAAG 1920
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1828 CTCCCTGACGACCTAATCAAGAGAGGCATGGCGGTCGCAGACCCGTCGAGCCCGTACAAG 1887
Qy 1921 GTACGGCTGCTGGTGGAGGACTACCCGTACGCGTCGGACGGGCTGGCCATCTGGCACGCC 1980
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1888 GTACGGCTGCTGGTGGAGGACTACCCGTACGCGTCGGACGGGCTGGCCATCTGGCACGCC 1947
Qy 1981 ATCGAGCAGTGGGTGACGGAGTACCTCGCCGTCTACTACCCCAACGACGGCGTGCTGCGG 2040
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1948 ATCGAGCAGTGGGTGACGGAGTACCTCGCCGTCTACTACCCCAACGACGGCGTGCTGCGG 2007
Qy 2041 GCGGACGTGGAGCTGCAGGCGTGGTGGAAGGAGGCGCGCGAGGTCGGGCACGCCGACCTC 2100
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2008 GCGGACGTGGAGCTGCAGGCGTGGTGGAAGGAGGCGCGCGAGGTCGGGCACGCCGACCTC 2067
Qy 2101 AAGGACGCGCCCTGGTGGCCCAAGATGCAGACGGTGGCCGAGCTGGTCAAGGCCTGCACC 2160
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2068 AAGGACGCGCCCTGGTGGCCCAAGATGCAGACGGTGGCCGAGCTGGTCAAGGCCTGCACC 2127
Qy 2161 ACCATCATCTGGATCGCGTCGGCGCTCCACGCGGCCGTCAACTTCGGGCAGTACCCGTAC 2220
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2128 ACCATCATCTGGATCGCGTCGGCGCTCCACGCGGCCGTCAACTTCGGGCAGTACCCGTAC 2187
Qy 2221 GCCGGGTACCTCCCGAACCGCCCGTCCGTCAGCCGGAAGCCGATGCCGGCGCCGGGCAGC 2280
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2188 GCCGGGTACCTCCCGAACCGCCCGTCCGTCAGCCGGAAGCCGATGCCGGCGCCGGGCAGC 2247
Qy 2281 GACGAGTACGCGGAGCTGGAGCGCAAGCCGGAGAAGGTGTTCGTGCGCACCATCACCAGC 2340
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2248 GACGAGTACGCGGAGCTGGAGCGCAAGCCGGAGAAGGTGTTCGTGCGCACCATCACCAGC 2307
Qy 2341 CAGTTCCAGGCCCTCGTCGGCATCTCGCTGCTGGAGATCCTGTCCAGCCACTCCTCCGAC 2400
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2308 CAGTTCCAGGCCCTCGTCGGCATCTCGCTGCTGGAGATCCTGTCCAGCCACTCCTCCGAC 2367
Qy 2401 GAGGTGTACCTCGGCCAGCGCGACACCAAGGAGTGGACGTCGGACGCCAAGGCGCAGGAG 2460
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2368 GAGGTGTACCTCGGCCAGCGCGACACCAAGGAGTGGACGTCGGACGCCAAGGCGCAGGAG 2427
Qy 2461 GCGTTCAAGCGGTTCGGCGCGCGGCTGACCGAGATCGAGAAACGCGTCGTCACCATGAAC 2520
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2428 GCGTTCAAGCGGTTCGGCGCGCGGCTGACCGAGATCGAGAAACGCGTCGTCACCATGAAC 2487
Qy 2521 GCGGACCCTCGCCTCAAGAACCGCAACGGCCCGGCCGAGTTCCCCTACACGCTGCTCTAC 2580
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2488 GCGGACCCTCGCCTCAAGAACCGCAACGGCCCGGCCGAGTTCCCCTACACGCTGCTCTAC 2547
Qy 2581 CCCAACACCTCCGACACGAAGGGCGACGCCGCCGGCATCACCGCCAAGGGCATTCCAAAC 2640
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2548 CCCAACACCTCCGACACGAAGGGCGACGCCGCCGGCATCACCGCCAAGGGCATTCCAAAC 2607
Qy 2641 AGCATCTCCATTTGA 2655
|||||||||||||||
Db 2608 AGCATCTCCATTTGA 2622
Against SEQ ID NO: 77
RESULT 1
A0A1D6N521_MAIZE
ID A0A1D6N521_MAIZE Unreviewed; 871 AA.
AC A0A1D6N521;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 28-JAN-2026, entry version 45.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=lox2 {ECO:0000313|EnsemblPlants:Zm00001eb144930_P002};
GN ORFNames=ZEAMMB73_Zm00001d042540 {ECO:0000313|EMBL:ONM35735.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ONM35735.1};
RN [1] {ECO:0000313|EMBL:ONM35735.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM35735.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:Zm00001eb144930_P002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb144930_P002};
RA Seetharam A., Woodhouse M., Cannon E.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:Zm00001eb144930_P002}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb144930_P002};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding.
CC {ECO:0000256|RuleBase:RU003975}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 = (9S)-hydroperoxy-(10E,12Z)-
CC octadecadienoate; Xref=Rhea:RHEA:30291, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:60955; EC=1.13.11.58;
CC Evidence={ECO:0000256|ARBA:ARBA00036508};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962,
CC ECO:0000256|RuleBase:RU003974};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000256|RuleBase:RU003975}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family.
CC {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003974}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM007649; ONM35735.1; -; Genomic_DNA.
DR RefSeq; NP_001105973.2; NM_001112503.2.
DR AlphaFoldDB; A0A1D6N521; -.
DR SMR; A0A1D6N521; -.
DR EnsemblPlants; Zm00001eb144930_T002; Zm00001eb144930_P002; Zm00001eb144930.
DR GeneID; 100037802; -.
DR Gramene; Zm00001eb144930_T002; Zm00001eb144930_P002; Zm00001eb144930.
DR KEGG; zma:100037802; -.
DR OrthoDB; 407298at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000007305; Chromosome 3.
DR ExpressionAtlas; A0A1D6N521; baseline and differential.
DR GO; GO:1990136; F:linoleate 9S-lipoxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0051707; P:response to other organism; IEA:UniProtKB-ARBA.
DR GO; GO:0009611; P:response to wounding; IEA:UniProtKB-ARBA.
DR CDD; cd01751; PLAT_LH2; 1.
DR FunFam; 1.20.245.10:FF:000002; Lipoxygenase; 1.
DR FunFam; 3.10.450.60:FF:000002; Lipoxygenase; 1.
DR FunFam; 4.10.372.10:FF:000001; Lipoxygenase; 1.
DR FunFam; 4.10.375.10:FF:000001; Lipoxygenase; 1.
DR Gene3D; 3.10.450.60; -; 1.
DR Gene3D; 4.10.375.10; Lipoxygenase-1, Domain 2; 1.
DR Gene3D; 4.10.372.10; Lipoxygenase-1, Domain 3; 1.
DR Gene3D; 1.20.245.10; Lipoxygenase-1, Domain 5; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR020833; LipOase_Fe_BS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR042057; Lipoxy_PLAT/LH2.
DR InterPro; IPR027433; Lipoxygenase_dom_3.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS00711; LIPOXYGENASE_1; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU003974};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU003975};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003974};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU003975};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003974};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003974};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW ECO:0000256|RuleBase:RU003975};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1D6N521};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT DOMAIN 35..166
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 169..871
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 213..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..242
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 98339 MW; D3F6F2AAD1B66765 CRC64;
Query Match 100.0%; Score 4647; Length 871;
Best Local Similarity 100.0%;
Matches 871; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MFGNIGKIPIIGDLTGSNKNAHLKGNLVLMRKTVLGFDVTSIAGSLMDGLGEFLGRGVTC 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MFGNIGKIPIIGDLTGSNKNAHLKGNLVLMRKTVLGFDVTSIAGSLMDGLGEFLGRGVTC 60
Qy 61 QLVSSTVVDPNNGNRGKVGQEASLEQWLLHPPPLLAGEDQFRVTFDWEVEKHGVPGAIIV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 QLVSSTVVDPNNGNRGKVGQEASLEQWLLHPPPLLAGEDQFRVTFDWEVEKHGVPGAIIV 120
Qy 121 KNNHASEFFLKTITIDDVPGHGPIVFVANSWVYPQYKYRYNRVFFSNDTYLPSQMPAALK 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 KNNHASEFFLKTITIDDVPGHGPIVFVANSWVYPQYKYRYNRVFFSNDTYLPSQMPAALK 180
Qy 181 PYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGNPDAKNPRPVLGGSKHHPYPRRGRT 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 PYRDDELRNLRGDDQQGPYQEHDRVYRYDVYNDLGNPDAKNPRPVLGGSKHHPYPRRGRT 240
Qy 241 GRKPTQTDPNSESRLTLTDGDVYVPRDERFGHIKNSDFYGYTIKAFVDGLVPILEGYLLG 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 GRKPTQTDPNSESRLTLTDGDVYVPRDERFGHIKNSDFYGYTIKAFVDGLVPILEGYLLG 300
Qy 301 IEFNSFKDILQLYEGGIKLPDIPALEEFRKQFPLQMVKDLMPAGGDYVLKLPMPKIIKED 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 IEFNSFKDILQLYEGGIKLPDIPALEEFRKQFPLQMVKDLMPAGGDYVLKLPMPKIIKED 360
Qy 361 KKAWMSDEEFARETLAGVNPLIIRRLTEFPPKSTLDPSKYGDQTSTITEAHIAGSLEGLT 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 KKAWMSDEEFARETLAGVNPLIIRRLTEFPPKSTLDPSKYGDQTSTITEAHIAGSLEGLT 420
Qy 421 VQQALDSNRLYILDHHDHYMPFLIEVNSLNDNFIYATRTLLFLRGDGTLAPVAIEMSLPE 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 VQQALDSNRLYILDHHDHYMPFLIEVNSLNDNFIYATRTLLFLRGDGTLAPVAIEMSLPE 480
Qy 481 LRDGITAAKSTVYTPAPPTAGAEAWVWRLAKAYVNVNDYCWHQGISHWLNTHAVMEPFVI 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 LRDGITAAKSTVYTPAPPTAGAEAWVWRLAKAYVNVNDYCWHQGISHWLNTHAVMEPFVI 540
Qy 541 ATNRQLSVTHPVHRLLLPHYRDTMNINALARQKLINAGGIFEMTVFPRKYAIEISSKVYG 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 ATNRQLSVTHPVHRLLLPHYRDTMNINALARQKLINAGGIFEMTVFPRKYAIEISSKVYG 600
Qy 601 SWNFTEQALPDDLIKRGMAVPDPSSPYKVRLLIEDYPYASDGLAVWHAIEQWVTEYLAIY 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 SWNFTEQALPDDLIKRGMAVPDPSSPYKVRLLIEDYPYASDGLAVWHAIEQWVTEYLAIY 660
Qy 661 YPNDGVLQADVELQAWWKEAREVGHADLKDEHWWPKMQTVPELVKACTTIIWIASALHAA 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 YPNDGVLQADVELQAWWKEAREVGHADLKDEHWWPKMQTVPELVKACTTIIWIASALHAA 720
Qy 721 VNFGQYPYCGYHPNRPSVSRRPMPVPGSDAYKELEKNPEKFFVRSITAQFQAVVGISLLE 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 VNFGQYPYCGYHPNRPSVSRRPMPVPGSDAYKELEKNPEKFFVRSITAQFQAVVGISLLE 780
Qy 781 ILSSHSSDEVYLGQRDTKEWTSDAKAQEAFKRFGARLTEIEKRVEAMNKDPRFKNRYSAA 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 ILSSHSSDEVYLGQRDTKEWTSDAKAQEAFKRFGARLTEIEKRVEAMNKDPRFKNRYSAA 840
Qy 841 QFPYTLLFPNTSDKGDNTGVTAKGIPNSISI 871
|||||||||||||||||||||||||||||||
Db 841 QFPYTLLFPNTSDKGDNTGVTAKGIPNSISI 871
Against SEQ ID NO: 83
RESULT 1
A1XCI1_MAIZE
ID A1XCI1_MAIZE Unreviewed; 892 AA.
AC A1XCI1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 28-JAN-2026, entry version 125.
DE RecName: Full=Lipoxygenase {ECO:0000256|RuleBase:RU003975};
DE EC=1.13.11.- {ECO:0000256|RuleBase:RU003975};
GN Name=LOX6 {ECO:0000313|EMBL:ABC59689.1};
GN Synonyms=lox6 {ECO:0000313|EnsemblPlants:Zm00001eb067710_P003};
GN ORFNames=ZEAMMB73_Zm00001d002000 {ECO:0000313|EMBL:ONM12732.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577 {ECO:0000313|EMBL:ABC59689.1};
RN [1] {ECO:0000313|EMBL:ABC59689.1}
RP NUCLEOTIDE SEQUENCE.
RA Kolomiets M.V., Navarro P., Nemchenko A., Simmons C., Davletova S.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABC59689.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=17922288; DOI=10.1007/s00425-007-0634-8;
RA Gao X., Stumpe M., Feussner I., Kolomiets M.;
RT "A novel plastidial lipoxygenase of maize (Zea mays) ZmLOX6 encodes for a
RT fatty acid hydroperoxide lyase and is uniquely regulated by phytohormones
RT and pathogen infection.";
RL Planta 227:491-503(2008).
RN [3] {ECO:0000313|EMBL:ACN28640.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B73 {ECO:0000313|EMBL:ACN28640.1};
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [4] {ECO:0000313|EMBL:ONM12732.1, ECO:0000313|Proteomes:UP000007305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|Proteomes:UP000007305};
RC TISSUE=Seedling {ECO:0000313|EMBL:ONM12732.1};
RG Maize Genome Sequencing Project;
RA Ware D.;
RT "Update maize B73 reference genome by single molecule sequencing
RT technologies.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EnsemblPlants:Zm00001eb067710_P003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb067710_P003};
RA Seetharam A., Woodhouse M., Cannon E.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EnsemblPlants:Zm00001eb067710_P003}
RP IDENTIFICATION.
RC STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb067710_P003};
RG EnsemblPlants;
RL Submitted (MAY-2021) to UniProtKB.
CC -!- FUNCTION: Plant lipoxygenase may be involved in a number of diverse
CC aspects of plant physiology including growth and development, pest
CC resistance, and senescence or responses to wounding.
CC {ECO:0000256|RuleBase:RU003975}.
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000256|RuleBase:RU003975}.
CC -!- SIMILARITY: Belongs to the lipoxygenase family.
CC {ECO:0000256|ARBA:ARBA00009419, ECO:0000256|RuleBase:RU003975}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ335764; ABC59689.1; -; mRNA.
DR EMBL; BT063943; ACN28640.1; -; mRNA.
DR EMBL; BT067473; ACN34370.1; -; mRNA.
DR EMBL; BT085507; ACR35860.1; -; mRNA.
DR EMBL; CM007648; ONM12732.1; -; Genomic_DNA.
DR RefSeq; NP_001105976.1; NM_001112506.1.
DR AlphaFoldDB; A1XCI1; -.
DR SMR; A1XCI1; -.
DR PaxDb; 4577-GRMZM2G040095_P02; -.
DR EnsemblPlants; Zm00001eb067710_T003; Zm00001eb067710_P003; Zm00001eb067710.
DR GeneID; 100037805; -.
DR Gramene; Zm00001eb067710_T003; Zm00001eb067710_P003; Zm00001eb067710.
DR KEGG; zma:100037805; -.
DR eggNOG; ENOG502QVKD; Eukaryota.
DR OrthoDB; 407298at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; A1XCI1; baseline and differential.
DR GO; GO:0009570; C:chloroplast stroma; IDA:AgBase.
DR GO; GO:0016832; F:aldehyde-lyase activity; IDA:AgBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0034440; P:lipid oxidation; IBA:GO_Central.
DR GO; GO:0042758; P:long-chain fatty acid catabolic process; IDA:AgBase.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009737; P:response to abscisic acid; IEP:AgBase.
DR GO; GO:0009723; P:response to ethylene; IEP:AgBase.
DR GO; GO:0009620; P:response to fungus; IEP:AgBase.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:AgBase.
DR GO; GO:0009751; P:response to salicylic acid; IEP:AgBase.
DR FunFam; 3.10.450.60:FF:000002; Lipoxygenase; 1.
DR Gene3D; 3.10.450.60; -; 1.
DR Gene3D; 4.10.375.10; Lipoxygenase-1, Domain 2; 1.
DR Gene3D; 1.20.245.10; Lipoxygenase-1, Domain 5; 1.
DR Gene3D; 2.60.60.20; PLAT/LH2 domain; 1.
DR InterPro; IPR000907; LipOase.
DR InterPro; IPR013819; LipOase_C.
DR InterPro; IPR036226; LipOase_C_sf.
DR InterPro; IPR020834; LipOase_CS.
DR InterPro; IPR001246; LipOase_plant.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR PANTHER; PTHR11771; LIPOXYGENASE; 1.
DR Pfam; PF00305; Lipoxygenase; 2.
DR PRINTS; PR00087; LIPOXYGENASE.
DR PRINTS; PR00468; PLTLPOXGNASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 1.
DR SUPFAM; SSF48484; Lipoxigenase; 1.
DR PROSITE; PS00081; LIPOXYGENASE_2; 1.
DR PROSITE; PS51393; LIPOXYGENASE_3; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160,
KW ECO:0000256|RuleBase:RU003975};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW ECO:0000256|RuleBase:RU003975};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Oxylipin biosynthesis {ECO:0000256|ARBA:ARBA00022767,
KW ECO:0000256|RuleBase:RU003975};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A1XCI1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT DOMAIN 70..201
FT /note="PLAT"
FT /evidence="ECO:0000259|PROSITE:PS50095"
FT DOMAIN 203..892
FT /note="Lipoxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51393"
FT REGION 265..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 97395 MW; 1F228A39232688A9 CRC64;
Query Match 100.0%; Score 4690; Length 892;
Best Local Similarity 100.0%;
Matches 892; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MMQQLRHSQPSPCLCGLRAARPMLALGAAASRSRPAGKLQPSVCLGLGHVAPAAARGQPR 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MMQQLRHSQPSPCLCGLRAARPMLALGAAASRSRPAGKLQPSVCLGLGHVAPAAARGQPR 60
Qy 61 PRAVADSALGASPTSVHVGGKLLLQNFAADSQQRLKLSIQLVSATVADPDGRGVKAEASV 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 PRAVADSALGASPTSVHVGGKLLLQNFAADSQQRLKLSIQLVSATVADPDGRGVKAEASV 120
Qy 121 LDAVVGSGDSELDVDLIWDEALGAPGAVVVKNHSDFPVYLRLLSVPAGVGGADDEAAAVH 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 LDAVVGSGDSELDVDLIWDEALGAPGAVVVKNHSDFPVYLRLLSVPAGVGGADDEAAAVH 180
Qy 181 FACNGWVYPVDKHPYRLFFTNDACVKEETPSALLKYREDELGALRGDGETTERPFQPWDR 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 FACNGWVYPVDKHPYRLFFTNDACVKEETPSALLKYREDELGALRGDGETTERPFQPWDR 240
Qy 241 VYDYALYNDLGNPDLRQDLARPVLGGSQEYPYPRRTKTGRPAAKTDPRSESRAPLDEEIY 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 VYDYALYNDLGNPDLRQDLARPVLGGSQEYPYPRRTKTGRPAAKTDPRSESRAPLDEEIY 300
Qy 301 VPCDERVGFASIPAPTLPPLGGHFRSLADVYRLFGLDDLGRLPEAKAVINSGAPFPVVPQ 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 VPCDERVGFASIPAPTLPPLGGHFRSLADVYRLFGLDDLGRLPEAKAVINSGAPFPVVPQ 360
Qy 361 VISVNPTHWRKDEEFARQMIAGANPVCIKRVTKFPLASELDRGVFGDQDSKITKDHVEKN 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 VISVNPTHWRKDEEFARQMIAGANPVCIKRVTKFPLASELDRGVFGDQDSKITKDHVEKN 420
Qy 421 MGGMTVQQAVEEGRLYVVDHHDWVMPYLKRINELPASEEKAEVSQRKVYAARTLLFLDGE 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 MGGMTVQQAVEEGRLYVVDHHDWVMPYLKRINELPASEEKAEVSQRKVYAARTLLFLDGE 480
Qy 481 DSSMLRPLAIELSSPHPEKEQLGAVSTVYTPPDSGDDGITAGRFSTWELAKVYASANDAA 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 DSSMLRPLAIELSSPHPEKEQLGAVSTVYTPPDSGDDGITAGRFSTWELAKVYASANDAA 540
Qy 541 ENNFVTHWLNTHASMEPIVIAANRQLSVLHPIHRLLKPHFRKTLHINAVARQIIVGSGDQ 600
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 ENNFVTHWLNTHASMEPIVIAANRQLSVLHPIHRLLKPHFRKTLHINAVARQIIVGSGDQ 600
Qy 601 RKDGSVFRGIDEVTYFPSKYNMEMSSKAYKAWNFTDLALPNDLIKRGLAKGDPKKPETVE 660
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 601 RKDGSVFRGIDEVTYFPSKYNMEMSSKAYKAWNFTDLALPNDLIKRGLAKGDPKKPETVE 660
Qy 661 LAIKDYPYAVDGLDMWAAIKKWVADYCAIYYADDGAVARDSELQGWWSEVRNVGHGDLAD 720
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 661 LAIKDYPYAVDGLDMWAAIKKWVADYCAIYYADDGAVARDSELQGWWSEVRNVGHGDLAD 720
Qy 721 APWWPAMDCVADLVETCATVVWLSSAYHASISFGQYDYLGFVPNGPSITTRPVPGPDAGA 780
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 721 APWWPAMDCVADLVETCATVVWLSSAYHASISFGQYDYLGFVPNGPSITTRPVPGPDAGA 780
Qy 781 EVTESDFLASVTPVTEALGFMSIASGPMGLKGTEVYLGQRPDTEQWTRERRAAEALAEFR 840
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 781 EVTESDFLASVTPVTEALGFMSIASGPMGLKGTEVYLGQRPDTEQWTRERRAAEALAEFR 840
Qy 841 ARLEEVAGNIDRRNADPALKNRTGQVEVPYTLLKPTAQPGLVLRGIPNSITV 892
||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 841 ARLEEVAGNIDRRNADPALKNRTGQVEVPYTLLKPTAQPGLVLRGIPNSITV 892
Response to Arguments
The application has been transferred to Examiner Wayne Zhong. In view of the significant amendment by the applicant, accordingly, the 102 rejection is withdrawn. the 103 rejections are rewritten.
Claims 15 and 62 are not rejected against prior art.
Thus, the arguments to the previous rejections are mostly not applicable.
For compact prosecution, the examiner would emphasize the following:
The focus of the applicant’s argument is that Gao et al do not teach or suggest making deletion mutations to maize LOX genes, and that the supporting references only teach deletion mutations, but do not teach the mutations are to LOX genes, and do not teach the deletion mutations are related to resistance to ear rot or stalk root.
The arguments are thoroughly analyzed and considered but are not deemed persuasive regarding the previous rejection by the previous examiner, or regarding the instant rejection.
Gao et al teach knocking out maize LOX genes, and demonstrate the result of conferring resistance to ear rot or stalk root.
The supporting references only need to teach that deletion, as a routine technique, is an alternative or functional equivalent to insertion or substitution mutations to edit or knockout a maize gene. The references clearly and thoroughly teach that.
If a supporting reference teaches that the mutations are to LOX genes, and that the deletion mutations lead to resistance to ear rot or stalk root, a 102 rejection would have been made.
In addition, the applicant admits that “other types of mutations useful for production of plants exhibiting increased resistance to ear rot and/or stalk rot include substitutions, deletions and insertions” (p40, 3rd para), and that “the edit results in a non-naturally occurring mutation, including but not limited to a deletion, substitution, or insertion, wherein the edit may result in a null allele or in a dominant negative mutation (p45, 3rd para).
Thus, by the teaching of prior art like Qi et al, and by the applicant’s own admission, deletion and substitution or insertion are functional equivalents in term of producing a gene editing, including a dominant negative mutation and increased resistance to ear rot and/or stalk rot.
Conclusion
Claims 1, 8, 12, 22, 24, 30, 34, 50, 56-57, 60-61, 84-86 are rejected.
Claims 15 and 62 are objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
The applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). The applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any extension fee pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action.
Contact information
Any inquiry concerning this communication or earlier communications from the examiner should be directed to WAYNE ZHONG whose telephone number is (571)270-0311. The examiner can normally be reached 8:30am to 5:00pm EST.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Bratislav Stankovic, can be reached on 571-270-0305. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/Wayne Zhong/
Primary Examiner, Art Unit 1662
Prosecution Insights