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 .
DETAILED ACTION
Applicant’s response filed on 06/22/2026 is duly acknowledged.
Claims 1-36 (originally presented) were previously canceled by applicants.
Claims 37-56 (newly presented) are pending in this application.
Election/Restrictions
Applicant’s election without traverse of Group I (Claims 37-49; directed to “A recombinant microorganism…” and “A method for producing a phenylpropanoid…”) in the reply filed on 06/22/2024 (see applicant’s REM, p. 1) is acknowledged.
Accordingly, claims 50-56 (non-elected invention of Group II) have been withdrawn from further considerations.
Claims 37-49 (elected invention of Group I, without traverse; directed to “A recombinant microorganism…” and “A method for producing a phenylpropanoid…”) as currently presented have been examined on their merits in this action hereinafter.
Priority
This application is a 371 of PCT/FR2022/052169 (filed on 11/23/2022), which claims foreign priority from a French application FR 2112410 filed on 11/23/2021.
Objection to Specification
The disclosure is objected to because it contains an embedded hyperlink and/or other form of browser-executable code (see SPEC, p. 8, lines 36-37). Applicant is required to delete the embedded hyperlink and/or other form of browser-executable code; references to websites should be limited to the top-level domain name without any prefix such as http:// or other browser-executable code. See MPEP § 608.01. Appropriate correction is required.
Claim Objections
1. Claims 38-41 and 43 (as presented) are objected to because of the following informalities: claims 38-41 and 43, each recite the limitations “one of these sequences” (see for instance claim 38-40, line 3), which should be amended to recite “one of said sequences” in order to clarify the invention as claimed. Appropriate correction is required.
2. Claim 42 (as presented) is objected to because of the following informalities: claim 42 recites limitations “CCR”, “ALDH” as abbreviations, which should be recited in full at least the first time they appear in a claim set. Appropriate correction is required.
Claim Rejections - 35 USC § 112
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 42 (as presented) is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention. Claim 42 has been reproduced as follows:
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It is noted that claim 42 recites that the recombinant microorganism “additionally comprises a heterologous nucleic acid sequence coding a CCR and a heterologous nucleic acid sequence coding for an ALDH” (see lines 2-3). However, it also recites the limitations for the same component genes with “and/or” later in lines 4-7, which is renders the claimed scope of the product ambiguous and confusing because, the metes and bounds of the claimed product can not be properly defined (also appears to have a broader as well as narrower limitations in the same claim). Appropriate correction is required.
Claim Rejections - 35 USC § 112 -WD issues
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 37-49 (as presented) are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the entire scope of the claimed invention.
A. Claims 37 and 48 recite the following:
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Regarding the term “microorganism”, the instant specification of record broadly states the following (see p. 7, lines 1-2):
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.
It is noted that the disclosure of record specifically pertains to construction and/or optimized expression of recombinant strains that belong to bacteria such as Escherichia coli and yeast such as Saccharomyces cerevisiae (see Examples 1-3, starting on p. 79). However, the term “microorganism” per se encompasses any type of prokaryotic and eukaryotic species of microbes, including variety of different bacterial species/strains, different species/strains of protozoa/protists, algal/diatoms/planktons species, just to name a few. It is also evident from the instant disclosure of record that even for the expression in specific strains of yeast as host cell (i.e. strains of Saccharomyces cerevisiae), applicants had to perform codon optimization of the gene constructs with various enzymes coded by heterologous nucleic acids as recited in the claims (see instant claim 37; and SPEC, p. 84, lines 2-3, for instance). The disclosure does not provide disclosure for any other recombinant “microorganism”, which would be encompassed by instant claim 37 as currently presented. The disclosure of a single species of yeast or bacterial strain would not be deemed sufficient written description to cover all the possible genera/species/strains of yeast, bacteria, or fungi, and other microorganisms that would be covered under the scope of the claims as currently presented by applicants. Thus, at the time this application was filed, applicant does not appear to have possession of the entire scope of the invention as claimed.
B. Claims 38-43 and 45 recite recombinant microorganism with various heterologous nucleic acid sequences coding for polypeptides (enzymes including 4-coumaroyl-CoA ligase, 4CL), coumaroyl-CoA 3-hydroxylase, CCoA3H, acyl-coenzyme A thioesterase, for instances) with limitations of “having at least 60% sequence identity” and exhibiting corresponding enzyme activities. The BRI of the claimed recombinant microorganism would encompass any derivative, variant, mutant (such as substitutions, deletions, truncations, etc.), or any other genetic alterations in the rest of 40% of the polypeptides as claimed. For example, the enzyme 4-coumaroyl-CoA ligase (4-CL) with SEQ ID NO: 5 as disclosed on record from Arabidopsis thaliana has a polypeptide length of 562 amino acids, a 40% of which would be about 225 amino acids of said polypeptide that can be altered, substituted with any of the 20 naturally occurring amino acids, or other type of genetic and/or chemical modifications, etc., and that resulting variant polypeptide would be required to express in a host cell, properly fold, and possess the same enzymatic and/or catalytic activity on its substrate(s). The disclosure of record does not provide for such variations in claimed enzyme polypeptide sequences that can be altered, mutated, and/or genetically changed in 40% of their amino acids in any location(s), and still remain active for the same type of catalytic activity. No such disclosure has been provided by applicants that would provide nexus with such a requirement as currently required by the aforementioned claims. Since, a single amino acid change in an enzyme at a catalytic location or site can destroy and/or substantially affect its activity on a given substrate, a change of 40% of the amino acids in polypeptide (with no disclosure for their location, domain, or any other information about the alterations, even for the 20 naturally occurring amino acids at each altered location in the polypeptides), would be deemed substantial absence of appropriate written description, at least for the variety of heterologous enzymes as currently being claimed for the product in the form of a recombinant microorganism (i.e. a host cell expressing said heterologous enzymes). Therefore, it is clear that applicants do not appear to be in possession of the entire scope of the invention as currently claimed. Appropriate correction is required.
NOTE: In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
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 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 nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 37-49 (as currently presented) are rejected under 35 U.S.C. 103 as being unpatentable over Zhang et al (2013; NPL cited in applicant’s IDS dated 05/23/2024, citation no. 6; complete NPL attached as ref. [V] on PTO 892 form) taken with Fojcik et al (US 2022/0372431 A1, US-PGPUB cited in IDS dated 05/23/2024; also published as WO 2021/089961 A1, FOR with publication date of 05/14/2021, also cited in IDS dated 05/23/2024) and Adebesin et al (2018; NPL cited as ref. [U] on PTO 892 form).
Claims 37 and 48 have been reproduced as follows:
“37 (new). A recombinant microorganism comprising a heterologous nucleic acid sequence coding a 4-coumaroyl-CoA ligase (4CL), a heterologous nucleic acid sequence coding a coumaroyl-CoA 3-hydroxylase (CCoA3H) and a heterologous nucleic acid sequence coding an acyl-coenzyme A thioesterase.”
“48 (new). A method for producing a phenylpropanoid chosen from caffeic acid and ferulic acid, comprising culturing a recombinant microorganism as claimed in claim 37 and optionally harvesting and/or purifying said phenylpropanoid.”
See also limitations of dependent claims 38-47 and 49, as currently presented.
Zhang et al (2013) disclose a genetically engineered Escherichia coli strain for biosynthesis of caffeic acid from tyrosine and/or from renewable sugars such as glucose (see Title, Abstract, Figure 1, Table 1, for instance). The Figure 1 on page 3334 discloses the following schematic for the caffeic acid biosynthesis pathway and responsible enzymes as reproduced below:
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The recombinant E. coli strain (regarding instant claim 37) comprises heterologous genes encoding a tyrosine ammonia lyase (TAL), a 4-coumarate-CoA ligase (4CL), and a 4-coumarate 3-hydroxylase (Coum3H) gene (see page 3335, left column, paragraph l; Table 1, strains RPC2 and RPC4). Since, Coum3H enzyme catalyzes the conversion of coumaroyl-CoA to caffeoyl-CoA (see page 3334, left-hand column, 2nd paragraph; and figure 1), it is taken as a coumaroyl-CoA 3- hydroxylase (CCoA3H) within the meaning of the present application (i.e. capable of producing caffeoyl-CoA from p-coumaroyl-CoA; see instant SPEC, page 14, lines 15-17). The TAL enzyme is derived from Rhodotorula glutinis (same source as instantly claimed TAL enzyme having SEQ ID NO: 19 in instant claim 45).
However, a recombinant microorganism that comprises (in addition to genes for 4CL and CCoA3H enzymes) a heterologous gene for Acyl-CoA thioesterase, has not been specifically exemplified by the teachings of Zhang et al, as discussed above.
Moreover, such incorporation of Acyl-CoA thioesterase gene in the E. coli strain disclosed by Zhang et al would have been obvious to an artisan of ordinary skill in the art because Zhang et al already suggests the fact that endogenous or heterologous caffeoyl-CoA thioesterase enzymes can be employed in order to enhance the production of caffeic acid (see Figure 1; and p. 3336, left column, 2nd paragraph; p. 3339, section “Discussion”, 1st paragraph). Since, Zhang et al explicitly disclose the fact that certain CoA thioesterases have been known to hydrolyze caffeoyl-CoA to make caffeic acid (see cited reference therein for Ramirez-AhumadaMdel et al, 2006; see p. 3334, left column, 2nd paragraph, in particular), such modification of the recombinant E. coli disclosed by Zhang et al would have been therefore obvious and/or fully contemplated by an artisan of ordinary skill in the art with a reasonable expectation of success, unless evidence/data provided on record to the contrary. In addition, since Zhang et al disclose the use of the recombinant E. coli strains having genes encoding 4CL, CCoA3H (and thioesterase endogenous to the host, that can also be incorporated using thioesterase genes from heterologous sources) to enhance the production of caffeic acid, the process as claimed in instant claim 48 would have been deemed obvious by an artisan of ordinary skill in the art, as discussed above before the effective filing date of the invention as currently claimed.
However, the recombinant microorganism wherein- the heterologous nucleic acid having at least 60% sequence identity and encoding a 4-coumaroyl-CoA ligase (4CL) with SEQ ID NOs: 5 to 9 (instant claim 38); wherein the “acyl-coenzyme A thioesterase comprises a sequence chosen from SEQ ID NOs: 1, 2 and 39…” (see instant claim 40); a caffeic acid O-methyltransferase (COMT) with SEQ ID NOs: 72 to 92 (instant claim 43); and wherein a “gene coding for a phenylpyruvate decarboxylase is inactivated and/or a gene coding for a ferulic acid decarboxylase is inactivated” (instant claim 47); have not been specifically exemplified or disclosed by Zhang et al, as discussed above.
Fojcik et al (2022; all citations per US-PGPUB ‘431), while teaching recombinant yeast having heterologous genes encoding enzymes capable of producing caffeic acid and/or ferulic acid (see Title, Abstract and Claims), disclose a 4-coumaroyl-CoA ligase (4CL) derived from the same source organism, Populus tomentosa (see [0049], Table 1, designated as SEQ ID NO: 10), as the 4CL having SEQ ID NO: 8 of instant claim 38; wherein they also disclose heterologous gene encoding a caffeic acid O-methyltransferase (COMT) enzyme from Arabidopsis thaliana (see [0115], Table 1, designated as SEQ ID NO: 2), which is the same source COMT as SEQ ID NO: 72 of instant claim 43; wherein a gene coding for a 3-deoxy-7-phosphoheptulonate synthase (ARO4) mutated so that the product is resistant to feedback inhibition compared to the parent gene, and/or a gene coding for a chorismate mutase (ARO7) mutated so that the product is resistant to feedback inhibition compared to the parent gene (instant claim 46; see Fojcik et al, [0087]-[0088]); wherein they disclose the yeast strain that is inactivated for phenylpyruvate decarboxylase (instant claim 47) by deletion of ARO10 gene YDR380W (see [0289]-[0290]; i.e. the same model yeast strain used by the applicants; see instant disclosure on p.80, 2nd paragraph); wherein they also disclose the expression of 4CL and COMT enzymes in combination with other enzymes in yeast (saccharomyces cerevisiae strains) required for the production of caffeic and/or ferulic acid (see Table 2 and Claims 8-17).
Also, regarding the specific acyl-CoA-thiotransferase (instant claim 40) as currently claimed, Adebesin et al (2018) already disclose such functional enzyme from Petunia hybrida which has a sequence identity of 98.9% to the claimed sequence of SEQ ID NO: 2 (see amino acid sequence homology reproduced below), and which has been known in the art for participation in the cytoplasmic phenylpropanoid biosynthetic pathway by catalyzing hydrolysis of aromatic acyl-CoAs to their corresponding acids (see Summary on p. 905, and Figure 1 schematic on p. 907; and p.915, section “Accession Numbers” for MF186602 and MF186603).
SEQ ID NO: 2 (Instant Claim 40; Acyl-CoA thioesterase)
RESULT 1 (UNIPROT database)
A0A2P1CQD7_PETHY
ID A0A2P1CQD7_PETHY Unreviewed; 164 AA.
AC A0A2P1CQD7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 10-JUN-2026, entry version 14.
DE SubName: Full=Thioesterase 1 {ECO:0000313|EMBL:AVK39784.1};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102 {ECO:0000313|EMBL:AVK39784.1};
RN [1] {ECO:0000313|EMBL:AVK39784.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29315918; DOI=10.1111/tpj.13818;
RA Adebesin F., Widhalm J.R., Lynch J.H., McCoy R., Dudareva N.;
RT "A peroxisomal thioesterase plays auxiliary roles in plant ?-oxidative
RT benzoic acid metabolism.";
RL Plant J. 93:905-916(2018).
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00060572}.
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 7/7.
CC {ECO:0000256|ARBA:ARBA00060586}.
CC -!- SUBUNIT: Homotetramers. {ECO:0000256|ARBA:ARBA00066058}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC DHNA-CoA hydrolase subfamily. {ECO:0000256|ARBA:ARBA00061187}.
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DR EMBL; MF186602; AVK39784.1; -; mRNA.
DR AlphaFoldDB; A0A2P1CQD7; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0061522; F:1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity; IEA:TreeGrafter.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-ARBA.
DR CDD; cd03443; PaaI_thioesterase; 1.
DR FunFam; 3.10.129.10:FF:000048; 14-dihydroxy-2-naphthoyl-CoA thioesterase 1; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR003736; PAAI_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR NCBIfam; TIGR00369; unchar_dom_1; 1.
DR PANTHER; PTHR43240; 1,4-DIHYDROXY-2-NAPHTHOYL-COA THIOESTERASE 1; 1.
DR PANTHER; PTHR43240:SF22; 1,4-DIHYDROXY-2-NAPHTHOYL-COA THIOESTERASE 1-LIKE; 1.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140}.
FT DOMAIN 52..121
FT /note="Thioesterase"
FT /evidence="ECO:0000259|Pfam:PF03061"
SQ SEQUENCE 164 AA; 17887 MW; B695D70A751CA004 CRC64;
Query Match 98.9%; Score 831; Length 164;
Best Local Similarity 100.0%;
Matches 163; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 3 KPPPLSSSAAGIKIREIDIPLHEIGFEYVEITPHKISGRLHLTERCCQPFKVLHGGISAL 62
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 KPPPLSSSAAGIKIREIDIPLHEIGFEYVEITPHKISGRLHLTERCCQPFKVLHGGISAL 61
Qy 63 IAESLASMGAHIASGFTRVAGVHLSIHHLKSAQLGDLVIAEAAPVNVGQSIQVWEVCLWK 122
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 62 IAESLASMGAHIASGFTRVAGVHLSIHHLKSAQLGDLVIAEAAPVNVGQSIQVWEVCLWK 121
Qy 123 IYESNEEEKKTLIASSRVTLKTNMFVPENAKDAAVVLKKYAKL 165
|||||||||||||||||||||||||||||||||||||||||||
Db 122 IYESNEEEKKTLIASSRVTLKTNMFVPENAKDAAVVLKKYAKL 164
Thus, given the detailed teachings in the cited prior art references of Zhang et al when taken with the disclosure from Fojcik et al and Adebesin et al, as discussed above, it would have been obvious to an artisan of ordinary skill in the art to modify the recombinant yeast or bacterial strains to incorporate the gene that express suitable acyl-CoA thioesterase (such as derived from Petunia hybrida, as taught by Adebesin et al, above) in order to enhance the production of caffeic acid as already suggested by Zhang et al. In addition, since, Fojcik et al already disclose the specific yeast strains that are deleted/inactivated for phenylpyruvate decarboxylase and disclose the required enzymes in the phenylpropanoid biosynthetic pathway for increased production of caffeic acid, such modifications in the recombinant yeast or bacterial strains would have been obvious and/or fully contemplated by an artisan in the art, unless evidence/data provided on record to the contrary (which is currently lacking in the disclosure of record commensurate with the scope of the currently claimed product).
It is also noted to applicants that the scope of the showing must be commensurate with the scope of claims to consider evidence probative of unexpected results, for example. In re Dill, 202 USPQ 805 (CCPA, 1979), In re Lindner 173 USPQ 356 (CCPA 1972), In re Hyson, 172 USPQ 399 (CCPA 1972), In re Boesch, 205 USPQ 215, (CCPA 1980), In re Grasselli, 218 USPQ 769 (Fed. Cir. 1983), In re Clemens, 206 USPQ 289 (CCPA 1980). It should be clear that the probative value of the data on record provided by applicants is not commensurate in scope with the degree of protection sought by the claim (see instant claim 37, in particular).
Thus, the claim as a whole would have been prima facie obvious to a person of ordinary skill in the art before the effective filing date of the invention as claimed.
As per MPEP 2111.01, during examination, the claims must be interpreted as broadly as their terms reasonably allow. In re American Academy of Science Tech Center, F.3d, 2004 WL 1067528 (Fed. Cir. May 13, 2004)(The USPTO uses a different standard for construing claims than that used by district courts; during examination the USPTO must give claims their broadest reasonable interpretation.). This means that the words of the claim must be given their plain meaning unless applicant has provided a clear definition in the specification. In re Zletz, 893 F.2d 319, 321, 13 USPQ2d 1320, 1322 (Fed. Cir. 1989).
Conclusion
NO claims are currently allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SATYENDRA K. SINGH whose telephone number is (571)272-8790. The examiner can normally be reached M-F 8:00- 5:00.
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, LOUISE W HUMPHREY can be reached at 571-272-5543. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
SATYENDRA K. SINGH
Primary Examiner
Art Unit 1657
/SATYENDRA K SINGH/Primary Examiner, Art Unit 1657
Enzymes in the prior art with more than 60% identity to claimed polypeptide sequences:
SEQ ID NO: 42 (Instant Claim 39, CCoA3H enzyme)
Results (Published database)
US-12-083-041-31
Filing date in PALM: 2009-02-27
Sequence 31, US/12083041
Publication No. US20090158456A1
GENERAL INFORMATION
APPLICANT: Cornell Research Foundation
APPLICANT: Nestec S.A.
APPLICANT: LEPELLEY, Maud
APPLICANT: CHEMINADE, Gerald
APPLICANT: MCCARTHY, James Gerard
APPLICANT: PETIARD, Vincent
APPLICANT: LIN, Chenwei
APPLICANT: TANKSLEY, Steven D.
TITLE OF INVENTION: Polynucleotides Encoding Phenylpropanoid Pathway Enzymes in
TITLE OF INVENTION: Coffee
FILE REFERENCE: 48520-1004 WO (NO7975/WO) (232313)
CURRENT APPLICATION NUMBER: US/12/083,041
CURRENT FILING DATE: 2008-04-15
PRIOR APPLICATION NUMBER: PCT/US2006/039618
PRIOR FILING DATE: 2006-10-10
PRIOR APPLICATION NUMBER: 60/724,673
PRIOR FILING DATE: 2006-10-07
NUMBER OF SEQ ID NOS: 90
SEQ ID NO 31
LENGTH: 509
TYPE: PRT
ORGANISM: Ocimum basilicum
ALIGNMENT:
Query Match 86.2%; Score 2317.5; Length 509;
Best Local Similarity 84.1%;
Matches 429; Conservative 46; Mismatches 34; Indels 1; Gaps 1;
Qy 1 MSALLLILPLSLITVWVAYTLYQRLSFKLPPGPRPWPVVGNLYDIKPVRFRCFAEWAQSY 60
|:||||:| | | ::: : || || |:||||||| ||||||||:|||||||||:|||||
Db 1 MAALLLLL-LLLPAIFLLHHLYYRLRFRLPPGPRPLPVVGNLYDVKPVRFRCFADWAQSY 59
Qy 61 GPIISVWFGSTLNVIVSNSELAKEVLKEQDQHLADRHRSRSAAKFSRDGKDLIWADYGPH 120
||||||||||||||||||:|||||||||:|| |||||||||||||||||:||||||||||
Db 60 GPIISVWFGSTLNVIVSNTELAKEVLKEKDQQLADRHRSRSAAKFSRDGQDLIWADYGPH 119
Qy 121 YVKVRKVCTLELFSPKRLEALRPIREDEVTAMVESIFHHCTTTENLGKGILVRKFLGEVA 180
|||||||| |||||||||||||||||||||||||||:| || :| || :||:|:|| ||
Db 120 YVKVRKVCMLELFSPKRLEALRPIREDEVTAMVESIYHDCTAPDNAGKSLLVKKYLGAVA 179
Qy 181 FNNITRLAFGKRFVNSEGVLEEQGVEFKGVVENGLKLGASLAMAEHIPWLRWMFPLEEEA 240
||||||||||||||||||::::||:||| :| ||||||||||||||||||||||||:|:|
Db 180 FNNITRLAFGKRFVNSEGIIDKQGLEFKAIVSNGLKLGASLAMAEHIPWLRWMFPLDEDA 239
Qy 241 FAKHGARRDRLTRAIMEEHTQARKKSGGAKQHFVDALLTLQDKYDLSEDTIIGLLWDMIT 300
|||||||||:||| ||||||:||::|||||||| ||||||:|||||||||||||||||||
Db 240 FAKHGARRDQLTREIMEEHTRAREESGGAKQHFFDALLTLKDKYDLSEDTIIGLLWDMIT 299
Qy 301 AGTDTSAISVEWAMAELIRNPRVQQKAQEELDRVIGLERVMTEADFLSLPYLQCVAKESL 360
|| ||:||||||||||||:||||||||||||||||| |||||| || :||||||||||:|
Db 300 AGMDTTAISVEWAMAELIKNPRVQQKAQEELDRVIGYERVMTELDFSNLPYLQCVAKEAL 359
Qy 361 RLHPPTPLMLPHRANANVKVGGYDIPKGSNVHVNVWAVARDPAVWKDPLEFRPERFLEED 420
|||||||||||||:|:|||:||||||||||||||||||||||||||:| |||||||||||
Db 360 RLHPPTPLMLPHRSNSNVKIGGYDIPKGSNVHVNVWAVARDPAVWKNPSEFRPERFLEED 419
Qy 421 VDMKGHDFRLLPFGAGRRVCPGAQLGINLVTSMLGHLLHHFSWNPAEGVKPEEIDMGENP 480
|||||||||||||||||||||||||||||||||:|||||||:| | || :|:||||||
Db 420 VDMKGHDFRLLPFGAGRRVCPGAQLGINLVTSMIGHLLHHFNWAPPSGVSTDELDMGENP 479
Qy 481 GLVTYMRTPLKGVPSPRLPSHLYKRLPADI 510
||||||||||: ||:||||| ||||: |:
Db 480 GLVTYMRTPLEAVPTPRLPSDLYKRIAVDL 509
SEQ ID NO: 42 (Instant Claim 39, CCoA3H)
RESULT 33 (A_Genseq database)
AFU68927
ID AFU68927 standard; protein; 509 AA.
XX
AC AFU68927;
XX
DT 14-JUN-2007 (first entry)
XX
DE Sweet basil C3H protein.
XX
KW crop improvement; flavor; aroma; prophylaxis; oxidative stress; enzyme;
KW C3H; p-coumaroyl 3' hydroxylase.
XX
OS Ocimum basilicum.
XX
CC PN WO2007044751-A2.
XX
CC PD 19-APR-2007.
XX
CC PF 10-OCT-2006; 2006WO-US039618.
XX
PR 07-OCT-2005; 2005US-0724673P.
XX
CC PA (CORR ) CORNELL RES FOUND INC.
CC PA (NEST ) NESTEC SA.
XX
CC PI Lepelley M, Cheminade G, Mccarthy JG, Petiard V, Lin C;
CC PI Tanksley SD;
XX
DR WPI; 2007-390431/36.
XX
CC PT New nucleic acid molecule isolated from coffee (Coffea spp.) having a
CC PT coding sequence that encodes a phenylpropanoid pathway enzyme, useful in
CC PT modulating flavor or aroma of coffee beans.
XX
CC PS Example 7; SEQ ID NO 31; 126pp; English.
XX
CC The invention describes a new nucleic acid molecule isolated from coffee
CC (Coffea spp.) having a coding sequence that encodes a phenylpropanoid
CC pathway enzyme (hydroxycinnamoyl-CoA shikimate/quinate
CC hydroxycinnamoyltansferase, hydroxycinnamoyl-CoA quinate
CC hydroxycinnamoyltransferase, p-coumaroyl 3' hydroxylase or caffeoyl-CoA 3
CC -O methyltransferase). The invention also includes: a mRNA molecule
CC produced by transcription of the gene; a cDNA molecule produced by
CC reverse transcription of the mRNA molecule; an oligonucleotide between 8
CC and 100 bases in length, which is complementary to a segment of the
CC nucleic acid molecule; a vector that comprises the coding sequence of the
CC nucleic acid molecule; a host cell transformed with the vector; a fertile
CC plant produced from the plant cell; a method of modulating flavor, aroma,
CC and other features of coffee beans; and polynucleotides and polypeptides
CC for protection or coffee plants against diseases or oxidative stress. The
CC nucleic acid molecule is useful in modulating flavor or aroma of coffee
CC beans. This sequence is a Sweet basil phenylpropanoid pathway enzyme-
CC related protein.
XX
SQ Sequence 509 AA;
Query Match 85.5%; Score 2298.5; Length 509;
Best Local Similarity 83.5%;
Matches 426; Conservative 47; Mismatches 36; Indels 1; Gaps 1;
Qy 1 MSALLLILPLSLITVWVAYTLYQRLSFKLPPGPRPWPVVGNLYDIKPVRFRCFAEWAQSY 60
|:||||:| | | ::: : || || |:||||||| ||||||||:|||||||||:|||||
Db 1 MAALLLLL-LLLPAIFLLHHLYYRLRFRLPPGPRPLPVVGNLYDVKPVRFRCFADWAQSY 59
Qy 61 GPIISVWFGSTLNVIVSNSELAKEVLKEQDQHLADRHRSRSAAKFSRDGKDLIWADYGPH 120
||||||||||||||||||:|||||||||:|| |||||||||||||||||:||||||||||
Db 60 GPIISVWFGSTLNVIVSNTELAKEVLKEKDQQLADRHRSRSAAKFSRDGQDLIWADYGPH 119
Qy 121 YVKVRKVCTLELFSPKRLEALRPIREDEVTAMVESIFHHCTTTENLGKGILVRKFLGEVA 180
|||||||| |||||||||||||||||||||||||||:| | :| || :||:|:|| ||
Db 120 YVKVRKVCMLELFSPKRLEALRPIREDEVTAMVESIYHDGTAPDNAGKSLLVKKYLGAVA 179
Qy 181 FNNITRLAFGKRFVNSEGVLEEQGVEFKGVVENGLKLGASLAMAEHIPWLRWMFPLEEEA 240
||||||||||||||||||::::||:||| :| ||||||||||||||||||||||||:|:|
Db 180 FNNITRLAFGKRFVNSEGIIDKQGLEFKAIVSNGLKLGASLAMAEHIPWLRWMFPLDEDA 239
Qy 241 FAKHGARRDRLTRAIMEEHTQARKKSGGAKQHFVDALLTLQDKYDLSEDTIIGLLWDMIT 300
|||||||||:||| :|||||:||::|||||||| ||||||:|||||||||||||||||||
Db 240 FAKHGARRDQLTRELMEEHTRAREESGGAKQHFFDALLTLKDKYDLSEDTIIGLLWDMIT 299
Qy 301 AGTDTSAISVEWAMAELIRNPRVQQKAQEELDRVIGLERVMTEADFLSLPYLQCVAKESL 360
|| ||:| ||||||||||:||||||||||||||||| |||||| || :||||||||||:|
Db 300 AGMDTTATSVEWAMAELIKNPRVQQKAQEELDRVIGYERVMTELDFSNLPYLQCVAKEAL 359
Qy 361 RLHPPTPLMLPHRANANVKVGGYDIPKGSNVHVNVWAVARDPAVWKDPLEFRPERFLEED 420
|||||||||||||:|:|||:||||||||||||||||||||||||||:| |||||||||||
Db 360 RLHPPTPLMLPHRSNSNVKIGGYDIPKGSNVHVNVWAVARDPAVWKNPSEFRPERFLEED 419
Qy 421 VDMKGHDFRLLPFGAGRRVCPGAQLGINLVTSMLGHLLHHFSWNPAEGVKPEEIDMGENP 480
|||||||||||||||||||||||||||||||||:|||||||:| | || :|:||||||
Db 420 VDMKGHDFRLLPFGAGRRVCPGAQLGINLVTSMIGHLLHHFNWAPPSGVSTDELDMGENP 479
Qy 481 GLVTYMRTPLKGVPSPRLPSHLYKRLPADI 510
||||||||||: ||:||||| ||||: |:
Db 480 GLVTYMRTPLEAVPTPRLPSDLYKRIAVDL 509
SEQ ID NO: 1 (Claim 40, Acyl-CoA Thioesterase)
RESULT 6 (Published database)
US-11-897-944-2047
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 2047, US/11897944
Publication No. US20080072340A1
GENERAL INFORMATION
APPLICANT: TROUKHAN, Maxim
APPLICANT: NAZDAN, Gregory
APPLICANT: MASCIA, Peter
APPLICANT: RARANG, Joel Cruz
APPLICANT: BURNS, James M.
APPLICANT: VOS STRACHE, Kyle
TITLE OF INVENTION: NUCLEOTIDE SEQUENCES AND CORRESPONDING POLYPEPTIDES CONFERRING
TITLE OF INVENTION: MODULATED PLANT CHARACTERISTICS
FILE REFERENCE: 2750-1694PUS2
CURRENT APPLICATION NUMBER: US/11/897,944
CURRENT FILING DATE: 2007-08-31
NUMBER OF SEQ ID NOS: 4192
SEQ ID NO 2047
LENGTH: 166
TYPE: PRT
ORGANISM: Populus balsamifera subsp. trichocarpa
FEATURE:
NAME/KEY: misc_feature
LOCATION: (1)..(166)
OTHER INFORMATION: Ceres ANNOT ID no. 1462354
FEATURE:
NAME/KEY: misc_feature
LOCATION: (52)..(129)
OTHER INFORMATION: Pfam Name: 4HBT
Pfam Description: Thioesterase superfamily
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: SWISSPROT Homolog: Y1161_HAEIN
Hypothetical UPF0152 protein HI1161
with e-value of 7.6e-14 and BLAST sequence identity of 37.7
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: SWISSPROT Homolog: Y3380_VIBCH
Hypothetical UPF0152 protein VCA0580
with e-value of 4.8e-12 and BLAST sequence identity of 30.0
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: SWISSPROT Homolog: YDII_ECOLI
Esterase ydiI
(EC 3.1.-.-)
with e-value of 7.8e-12 and BLAST sequence identity of 30.1
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: SWISSPROT Homolog: Y1618_PSEAE
Hypothetical UPF0152 protein PA1618
with e-value of 1.3e-11 and BLAST sequence identity of 33.7
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: SWISSPROT Homolog: Y788_PASMU
Hypothetical UPF0152 protein PM0788
with e-value of 7.0e-11 and BLAST sequence identity of 33.6
FEATURE:
NAME/KEY: misc_feature
LOCATION: 229138:<222
OTHER INFORMATION: Transcription Factor
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: WHOLE PLANT - Dark Green
Useful for increasing chlorophyll and photosynthetic capacity
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: ROSETTE LEAVES - Disorganized Rosette
Useful for making plants with increased biomass
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: WHOLE PLANT - Small
Useful for modulating plant size
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: WHOLE PLANT - Yellow-Green Viable 2
Useful for making lethal plants for genetic confinement systems
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: WHOLE PLANT - High Anthocyanin
Useful for modulating anthocyanin content
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: INFLORESCENCE - Reduced Apical Dominance
Useful for modifying plant structure, ie increased branching
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: INFLORESCENCE - Other
Useful for making ornamental plants with modified flowers
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: ROSETTE LEAVES - Other
Useful for making ornamental plants with modified leaves
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: ROSETTE LEAVES - Oval Shaped
Useful for making plants with increased biomass and foliage
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: ROSETTE LEAVES - Ovate Shaped
Useful for making plants with increased biomass and foliage
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: ROSETTE LEAVES - Serrate Margins
Useful for making plants with increased biomass and foliage
FEATURE:
NAME/KEY: misc_feature
LOCATION:
OTHER INFORMATION: Phenotype: ROSETTE LEAVES - Trident Shaped
Useful for making plants with increased biomass and foliage
FEATURE:
NAME/KEY: misc_feature
LOCATION: (1)..(166)
OTHER INFORMATION: Functional Homolog of Ceres CLONE ID no. 42925
at SEQ ID NO. 2089
with e-value of 5.30E-51 and BLAST sequence identity of 66.2
Query Match 66.6%; Score 531; Length 166;
Best Local Similarity 65.2%;
Matches 103; Conservative 25; Mismatches 28; Indels 2; Gaps 1;
Qy 2 SDSASSNTKAIDPPLHMLGFEFDELSPTRITGRLPVSPVCCQPFKVLHGGVSALIAESLA 61
| |:|| :::| ||| ||: :|||| ::|||| |:| | ||||||||||||||:|::|
Db 9 SSSSSSKKESLDVPLHSFGFQIEELSPQKVTGRLLVTPKCVQPFKVLHGGVSALISEAMA 68
Qy 62 SMGAHMASGFKRVAGIQLSINHLKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTT--QK 119
||||||||| :||||| |||||:||| ||||| ||||| | |||||||||::||
Db 69 SMGAHMASGLQRVAGIHLSINHVKSARLGDLVLAEATPFSIGKTIQVWEVRIWKLADPSN 128
Qy 120 DKANKILISSSRVTLICNLPIPDNAKDAANMLKMVAKL 157
:::| |:|||||||:||||:||:||:| |: |||
Db 129 TESSKSLVSSSRVTLMCNLPVPDHAKEATENLRSHAKL 166
SEQ ID NO: 1 (Instant Claim 40; Acyl-CoA thioesterase)
RESULT 1 (UNIPROT database)
A0A8T2GNM1_9BRAS
ID A0A8T2GNM1_9BRAS Unreviewed; 156 AA.
AC A0A8T2GNM1;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 10-JUN-2026, entry version 14.
DE SubName: Full=Thioesterase domain {ECO:0000313|EMBL:KAG7648935.1};
GN ORFNames=ISN45_At01g040230 {ECO:0000313|EMBL:KAG7648935.1};
OS Arabidopsis thaliana x Arabidopsis arenosa.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=1240361 {ECO:0000313|EMBL:KAG7648935.1, ECO:0000313|Proteomes:UP000694240};
RN [1] {ECO:0000313|EMBL:KAG7648935.1, ECO:0000313|Proteomes:UP000694240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Allo738 {ECO:0000313|EMBL:KAG7648935.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG7648935.1};
RA Chen Z.;
RT "Concerted genomic and epigenomic changes stabilize Arabidopsis
RT allopolyploids.";
RL Submitted (DEC-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; phylloquinone biosynthesis.
CC {ECO:0000256|ARBA:ARBA00060572}.
CC -!- PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate
CC biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 7/7.
CC {ECO:0000256|ARBA:ARBA00060586}.
CC -!- SUBUNIT: Homotetramers. {ECO:0000256|ARBA:ARBA00066058}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC DHNA-CoA hydrolase subfamily. {ECO:0000256|ARBA:ARBA00061187}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG7648935.1}.
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DR EMBL; JAEFBK010000001; KAG7648935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8T2GNM1; -.
DR SMR; A0A8T2GNM1; -.
DR Proteomes; UP000694240; Chromosome 1.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0061522; F:1,4-dihydroxy-2-naphthoyl-CoA thioesterase activity; IEA:TreeGrafter.
DR GO; GO:0042372; P:phylloquinone biosynthetic process; IEA:UniProtKB-ARBA.
DR CDD; cd03443; PaaI_thioesterase; 1.
DR FunFam; 3.10.129.10:FF:000048; 14-dihydroxy-2-naphthoyl-CoA thioesterase 1; 1.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR003736; PAAI_dom.
DR InterPro; IPR006683; Thioestr_dom.
DR NCBIfam; TIGR00369; unchar_dom_1; 1.
DR PANTHER; PTHR43240; 1,4-DIHYDROXY-2-NAPHTHOYL-COA THIOESTERASE 1; 1.
DR PANTHER; PTHR43240:SF5; 1,4-DIHYDROXY-2-NAPHTHOYL-COA THIOESTERASE 1; 1.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000694240}.
FT DOMAIN 45..118
FT /note="Thioesterase"
FT /evidence="ECO:0000259|Pfam:PF03061"
SQ SEQUENCE 156 AA; 16713 MW; 986C79FC0F985B23 CRC64;
Query Match 98.9%; Score 788; Length 156;
Best Local Similarity 100.0%;
Matches 155; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 3 DSASSNTKAIDPPLHMLGFEFDELSPTRITGRLPVSPVCCQPFKVLHGGVSALIAESLAS 62
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 DSASSNTKAIDPPLHMLGFEFDELSPTRITGRLPVSPVCCQPFKVLHGGVSALIAESLAS 61
Qy 63 MGAHMASGFKRVAGIQLSINHLKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTQKDKA 122
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 62 MGAHMASGFKRVAGIQLSINHLKSADLGDLVFAEATPVSTGKTIQVWEVKLWKTTQKDKA 121
Qy 123 NKILISSSRVTLICNLPIPDNAKDAANMLKMVAKL 157
|||||||||||||||||||||||||||||||||||
Db 122 NKILISSSRVTLICNLPIPDNAKDAANMLKMVAKL 156
SEQ ID NO: 10 (Instant claim 41; Caffeoyl-CoA-methyltransferase, CCoAMT)
RESULT 1 (UNIPROT DATABASE)
CAMT_VITVI
ID CAMT_VITVI Reviewed; 242 AA.
AC Q43237;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 10-JUN-2026, entry version 110.
DE RecName: Full=Caffeoyl-CoA O-methyltransferase;
DE EC=2.1.1.104;
DE AltName: Full=Trans-caffeoyl-CoA 3-O-methyltransferase;
DE Short=CCOAMT;
DE Short=CCOAOMT;
OS Vitis vinifera (Grape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; Vitales; Vitaceae; Viteae; Vitis.
OX NCBI_TaxID=29760;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9390437; DOI=10.1104/pp.115.3.1039;
RA Busam G., Junghanns K.T., Kneusel R.E., Kassemeyer H.H., Matern U.;
RT "Characterization and expression of caffeoyl-coenzyme A 3-O-
RT methyltransferase proposed for the induced resistance response of Vitis
RT vinifera L.";
RL Plant Physiol. 115:1039-1048(1997).
CC -!- FUNCTION: Methylates caffeoyl-CoA to feruloyl-CoA and 5-
CC hydroxyferuloyl-CoA to sinapoyl-CoA. Plays a role in the synthesis of
CC feruloylated polysaccharides. Involved in the reinforcement of the
CC plant cell wall. Also involved in the responding to wounding or
CC pathogen challenge by the increased formation of cell wall-bound
CC ferulic acid polymers.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeoyl-CoA + S-adenosyl-L-methionine = (E)-feruloyl-CoA
CC + S-adenosyl-L-homocysteine + H(+); Xref=Rhea:RHEA:16925,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:87136, ChEBI:CHEBI:87305; EC=2.1.1.104;
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q40313};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:Q40313};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family. CCoAMT
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; Z54233; CAA90969.1; -; mRNA.
DR RefSeq; NP_001268047.1; NM_001281118.1.
DR AlphaFoldDB; Q43237; -.
DR SMR; Q43237; -.
DR GeneID; 100233087; -.
DR KEGG; vvi:100233087; -.
DR eggNOG; KOG1663; Eukaryota.
DR OrthoDB; 163365at71240; -.
DR BRENDA; 2.1.1.104; 6671.
DR UniPathway; UPA00711; -.
DR GO; GO:0042409; F:caffeoyl-CoA O-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR FunFam; 3.40.50.150:FF:000147; Caffeoyl-CoA O-methyltransferase 1; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR050362; Cation-dep_OMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR PANTHER; PTHR10509:SF81; CAFFEOYL-COA O-METHYLTRANSFERASE 1; 1.
DR PANTHER; PTHR10509; O-METHYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 2: Evidence at transcript level;
KW Lignin biosynthesis; Metal-binding; Methyltransferase;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..242
FT /note="Caffeoyl-CoA O-methyltransferase"
FT /id="PRO_0000165703"
FT BINDING 16
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 82..83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 88
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 106
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 158
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 158
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
FT BINDING 160
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 184
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 185
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q40313"
SQ SEQUENCE 242 AA; 27234 MW; 6BBAA5E5BBE65F2A CRC64;
Query Match 99.3%; Score 1258; Length 242;
Best Local Similarity 100.0%;
Matches 241; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 3 ATNQEAGRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAQHPWNIMTTSAD 62
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 ATNQEAGRHQEVGHKSLLQSDALYQYILETSVYPREPESMKELRELTAQHPWNIMTTSAD 61
Qy 63 EGQFLNMLLKLINAKNTMEIGVYTGYSLLATALALPDDGKILAMDINKENYELGLPVIQK 122
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 62 EGQFLNMLLKLINAKNTMEIGVYTGYSLLATALALPDDGKILAMDINKENYELGLPVIQK 121
Qy 123 AGVAHKIDFKEGPALPVLDQMIEDGKYHGSFDFIFVDADKDNYLNYHKRLIDLVKVGGII 182
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 122 AGVAHKIDFKEGPALPVLDQMIEDGKYHGSFDFIFVDADKDNYLNYHKRLIDLVKVGGII 181
Qy 183 GYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITLCRRL 242
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 182 GYDNTLWNGSVVAPPDAPLRKYVRYYRDFVLELNKALAADPRIEICMLPVGDGITLCRRL 241
Qy 243 S 243
|
Db 242 S 242
SEQ ID NO: 3 (Instant claim 42; ALDH)
AAY67413 (UNIPROT database)
ID AAY67413 standard; protein; 501 AA.
XX
AC AAY67413;
XX
DT 15-JUN-2007 (revised)
DT 12-MAY-2000 (first entry)
XX
DE Arabidopsis aldehyde dehydrogenase (ALDH)-2.
XX
KW Arabidopsis; plant plastid; acetyl CoA synthetase; E3 subunit; ACS;
KW plant plastidic pyruvate dehydrogenase; pPDH; ATP citrate lyase; ACL;
KW pyruvate decarboxylase; PDC; aldehyde dehydrogenase; ALDH; acetyl CoA;
KW fatty acid; flavonoid; enzyme; phytochemical; pyruvate decarboxylase;
KW acetyl CoA hydrolase; mitochondrial pyruvate dehydrogenase; BOND_PC;
KW aldehyde dehydrogenase (ALDH1a);
KW aldehyde dehydrogenase (ALDH1a) [Arabidopsis thaliana]; MOB24.3; ALDH2C4;
KW ALDH1A, REDUCED EPIDERMAL FLUORESCENCE1, REF1; aldehyde dehydrogenase;
KW aldehyde dehydrogenase [Arabidopsis thaliana];
KW aldehyde dehydrogenase ALDH1a;
KW aldehyde dehydrogenase ALDH1a [Arabidopsis thaliana].
XX
OS Arabidopsis sp.
XX
CC PN WO200000619-A2.
XX
CC PD 06-JAN-2000.
XX
CC PF 25-JUN-1999; 99WO-US014382.
XX
PR 26-JUN-1998; 98US-0090717P.
XX
CC PA (IOWA ) UNIV IOWA STATE RES FOUND INC.
XX
CC PI Nikolau BJ, Wurtele ES, Oliver DJ, Behal R, Schnable PS, Ke J;
CC PI Johnson JL, Allred CC, Fatland B, Lutziger I, Wen T;
XX
DR WPI; 2000-160678/14.
DR N-PSDB; AAZ56974.
DR PC:NCBI; gi9294041.
DR PC:SWISSPROT; Q56YU0.
XX
CC PT Novel acetyl CoA synthetase (ACS), plastidic pyruvate dehydrogenase
CC PT (pPDH), ATP citrate lyase (ACL), pyruvate decarboxylase (PDC) and
CC PT aldehyde dehydrogenase (ALDH) polypeptides used to alter acetyl CoA
CC PT levels in plants.
XX
CC PS Claim 30; Fig 11B; 79pp; English.
XX
CC The invention provides nucleic acids encoding Arabidopsis plastidic
CC acetyl CoA synthetase (ACS), various subunits (specifically the E3
CC subunit) of plant plastidic pyruvate dehydrogenase (pPDH), the A and B
CC subunits of a plant ATP citrate lyase (ACL), Arabidopsis pyruvate
CC decarboxylase (PDC), Arabidopsis aldehyde dehydrogenase (ALDH),
CC specifically ALDH-2 and ALDH-4. The polypeptides can be expressed by
CC standard recombinant methodology. The ACS, pPDH, ACL, PDC and ALDH
CC polypeptides, methods and nucleic acid molecules of the invention are
CC used to alter the level of acetyl CoA in a plant or plant cell, tissues
CC or organs. A decrease in acetyl CoA is expected to affect the
CC biosynthesis of very long chain fatty acids and flavonoids. The enzymes
CC may also be used for in vitro synthesis of acetyl CoA, which in turn can
CC be used to produce acetyl CoA phytochemicals (plastidic ACS, pPDH, ACL,
CC pyruvate decarboxylase, acetyl CoA hydrolase, mitochondrial pyruvate
CC dehydrogenase and aldehyde dehydrogenase are involved in the biosynthesis
CC of acetyl CoA
CC
CC Revised record issued on 15-JUN-2007 : Enhanced with precomputed
CC information from BOND.
XX
SQ Sequence 501 AA;
Query Match 99.7%; Score 2601; Length 501;
Best Local Similarity 100.0%;
Matches 500; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 3 ENGKCNGATTVKLPEIKFTKLFINGQFIDAASGKTFETIDPRNGEVIATIAEGDKEDVDL 62
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 ENGKCNGATTVKLPEIKFTKLFINGQFIDAASGKTFETIDPRNGEVIATIAEGDKEDVDL 61
Qy 63 AVNAARYAFDHGPWPRMTGFERAKLINKFADLIEENIEELAKLDAVDGGKLFQLGKYADI 122
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 62 AVNAARYAFDHGPWPRMTGFERAKLINKFADLIEENIEELAKLDAVDGGKLFQLGKYADI 121
Qy 123 PATAGHFRYNAGAADKIHGETLKMTRQSLFGYTLKEPIGVVGNIIPWNFPSIMFATKVAP 182
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 122 PATAGHFRYNAGAADKIHGETLKMTRQSLFGYTLKEPIGVVGNIIPWNFPSIMFATKVAP 181
Qy 183 AMAAGCTMVVKPAEQTSLSALFYAHLSKEAGIPDGVLNIVTGFGSTAGAAIA SHMDVDKV 242
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 182 AMAAGCTMVVKPAEQTSLSALFYAHLSKEAGIPDGVLNIVTGFGSTAGAAIA SHMDVDKV 241
Qy 243 SFTGSTDVGRKIMQAAAASNLKKVSLELGGKSPLLIFNDADIDKAADLALLGCFYNKGEI 302
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 242 SFTGSTDVGRKIMQAAAASNLKKVSLELGGKSPLLIFNDADIDKAADLALLGCFYNKGEI 301
Qy 303 CVASSRVFVQEGIYDKVVEKLVEKAKDWTVGDPFDSTARQGPQVDKRQFEKILSYIEHGK 362
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 302 CVASSRVFVQEGIYDKVVEKLVEKAKDWTVGDPFDSTARQGPQVDKRQFEKILSYIEHGK 361
Qy 363 NEGATLLTGGKAIGDKGYFIQPTIFADVTEDMKIYQDEIFGPVMSLMKFKTVEEGIKCAN 422
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 362 NEGATLLTGGKAIGDKGYFIQPTIFADVTEDMKIYQDEIFGPVMSLMKFKTVEEGIKCAN 421
Qy 423 NTKYGLAAGILSQDIDLINTVSRSIKAGIIWVNCYFGFDLDCPYGGYKMSGNCRESGMDA 482
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 422 NTKYGLAAGILSQDIDLINTVSRSIKAGIIWVNCYFGFDLDCPYGGYKMSGNCRESGMDA 481
Qy 483 LDNYLQTKSVVMPLHNSPWM 502
||||||||||||||||||||
Db 482 LDNYLQTKSVVMPLHNSPWM 501
SEQ ID NO: 4 (Instant claim 42; Cinnamoyl-CoA Reductase, CCR)
RESULT 1 (Uniprot database)
A0A0F7EVN0_POPTO
ID A0A0F7EVN0_POPTO Unreviewed; 341 AA.
AC A0A0F7EVN0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 28-JAN-2026, entry version 27.
DE RecName: Full=cinnamoyl-CoA reductase {ECO:0000256|ARBA:ARBA00067006};
DE EC=1.2.1.44 {ECO:0000256|ARBA:ARBA00067006};
DE AltName: Full=Caffeoyl-CoA reductase {ECO:0000256|ARBA:ARBA00075244};
DE AltName: Full=Coumaroyl-CoA reductase {ECO:0000256|ARBA:ARBA00082321};
DE AltName: Full=Feruloyl-CoA reductase {ECO:0000256|ARBA:ARBA00077069};
DE AltName: Full=Sinapoyl-CoA reductase {ECO:0000256|ARBA:ARBA00081990};
OS Populus tomentosa (Chinese white poplar).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=118781 {ECO:0000313|EMBL:AKG06582.1};
RN [1] {ECO:0000313|EMBL:AKG06582.1}
RP NUCLEOTIDE SEQUENCE.
RA Li N., Chao N., Gai Y., Jiang X.;
RT "Key gene involved in lignin biosynthesis.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-4-coumaraldehyde + NADP(+) + CoA = (E)-4-coumaroyl-CoA +
CC NADPH + H(+); Xref=Rhea:RHEA:64652, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28353, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:85008; EC=1.2.1.44;
CC Evidence={ECO:0000256|ARBA:ARBA00050640};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64654;
CC Evidence={ECO:0000256|ARBA:ARBA00050640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-caffeyl aldehyde + NADP(+) + CoA = (E)-caffeoyl-CoA +
CC NADPH + H(+); Xref=Rhea:RHEA:74867, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28323, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:87136;
CC Evidence={ECO:0000256|ARBA:ARBA00051239};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:74869;
CC Evidence={ECO:0000256|ARBA:ARBA00051239};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamaldehyde + NADP(+) + CoA = (E)-cinnamoyl-CoA + NADPH
CC + H(+); Xref=Rhea:RHEA:10620, ChEBI:CHEBI:15378, ChEBI:CHEBI:16731,
CC ChEBI:CHEBI:57252, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.44;
CC Evidence={ECO:0000256|ARBA:ARBA00050514};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10622;
CC Evidence={ECO:0000256|ARBA:ARBA00050514};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferaldehyde + NADP(+) + CoA = (E)-feruloyl-CoA + NADPH
CC + H(+); Xref=Rhea:RHEA:64648, ChEBI:CHEBI:15378, ChEBI:CHEBI:16547,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:87305; EC=1.2.1.44;
CC Evidence={ECO:0000256|ARBA:ARBA00052462};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64650;
CC Evidence={ECO:0000256|ARBA:ARBA00052462};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-sinapaldehyde + NADP(+) + CoA = (E)-sinapoyl-CoA + NADPH +
CC H(+); Xref=Rhea:RHEA:64656, ChEBI:CHEBI:15378, ChEBI:CHEBI:27949,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57393, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.44;
CC Evidence={ECO:0000256|ARBA:ARBA00051133};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64658;
CC Evidence={ECO:0000256|ARBA:ARBA00051133};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004928}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. Dihydroflavonol-4-reductase subfamily.
CC {ECO:0000256|ARBA:ARBA00023445}.
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DR EMBL; KP281597; AKG06582.1; -; mRNA.
DR AlphaFoldDB; A0A0F7EVN0; -.
DR BRENDA; 1.2.1.44; 8103.
DR GO; GO:0016621; F:cinnamoyl-CoA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:TreeGrafter.
DR GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-ARBA.
DR CDD; cd08958; FR_SDR_e; 1.
DR FunFam; 3.40.50.720:FF:000199; Cinnamoyl-CoA reductase 1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR050425; NAD(P)_dehydrat-like.
DR PANTHER; PTHR10366:SF404; CINNAMOYL-COA REDUCTASE 1; 1.
DR PANTHER; PTHR10366; NAD DEPENDENT EPIMERASE/DEHYDRATASE; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 15..247
FT /note="NAD-dependent epimerase/dehydratase"
FT /evidence="ECO:0000259|Pfam:PF01370"
SQ SEQUENCE 341 AA; 37541 MW; 61AB7A5E2AA130FC CRC64;
Query Match 99.5%; Score 1786; Length 341;
Best Local Similarity 100.0%;
Matches 340; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 3 PVDISSLPCQGQTVCVTGAGGFIASWIVKLLLEKGYSVKGTVRNPADPKNSHLRELEGAQ 62
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 2 PVDISSLPCQGQTVCVTGAGGFIASWIVKLLLEKGYSVKGTVRNPADPKNSHLRELEGAQ 61
Qy 63 ERLTLCKADILDYESLKMAIQGCDGVFHTACPITDDPDMVMAPAVNGTKNVIMAAAETKV 122
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 62 ERLTLCKADILDYESLKMAIQGCDGVFHTACPITDDPDMVMAPAVNGTKNVIMAAAETKV 121
Qy 123 RRVVVTSSIGTVYMDPNRSPDVVVDESCWSDLEFCKSTKNWYCYGRTVAEQVAWDVAKKK 182
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 122 RRVVVTSSIGTVYMDPNRSPDVVVDESCWSDLEFCKSTKNWYCYGRTVAEQVAWDVAKKK 181
Qy 183 GVDLVVVNPVMVLGPLLQPTVNASIGHILKYLTGSAKTYANSVQAYVHVRDVALAHILVF 242
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 182 GVDLVVVNPVMVLGPLLQPTVNASIGHILKYLTGSAKTYANSVQAYVHVRDVALAHILVF 241
Qy 243 ETPSASGRYICAERMLHRGEVVEILAKFFPEYPIPTKCSDEKNPRKQPYKFTNQKIKDLG 302
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 242 ETPSASGRYICAERMLHRGEVVEILAKFFPEYPIPTKCSDEKNPRKQPYKFTNQKIKDLG 301
Qy 303 IEFTPVKQCLYETVKSLQEKGHLPIPKQAQDSSVVGISKY 342
||||||||||||||||||||||||||||||||||||||||
Db 302 IEFTPVKQCLYETVKSLQEKGHLPIPKQAQDSSVVGISKY 341
Prosecution Insights