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 04/16/2026 is duly acknowledged.
Claims 3, 6-8, 10, 13, 15-23, 25, 27, 29, 33-41, 43-45, 47, 48, 51-53, 56 and 58 have been canceled by applicants.
Claims 1, 2, 4, 5, 9, 11, 12, 14, 24, 26, 28, 30-32, 42, 46, 49, 50, 54, 55 and 57, as currently amended/presented, are pending in this application.
Election/Restrictions
Applicant's election with traverse of Group I (Species A from claim 5; directed to “An engineered formate dehydrogenase comprising a variant of amino acid sequence SEQ ID NO: 1…comprises a substitution at a residue corresponding to position 266 in SEQ ID NO: 1”) in the reply filed on 04/16/2026 (see REM, p. 10-12) is acknowledged (elected Species A reads on instant claims 1, 2, 4, 5, 9, 11, 12, 14, 24 and 26, as per applicant’s election; see REM, p. 12, last paragraph). The traversal is mainly on the ground(s) stated by applicants as follows:
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The traversal is duly noted and considered. However, this is not found persuasive because as noted in the previous office action (see CTRS dated 02/05/2026, p. 4-5), since the common technical feature of the claimed inventions still pertains to a bioderived compound, or composition thereof (group V, claim 42), which still remain the same irrespective of the current claim amendments as currently presented (the change in the extent and/or degree of enzyme activity, imparted by certain mutations, would not be deemed to structurally alter and/or change the resulting product/bioderived compound, as per applicant’s disclosure of record at p. 101, Table 6), the disclosure in the cited reference of Park et al (US 9,920,325 B2) is still pertinent, and therefore, the inventions lack unity a posteriori.
The requirement is still deemed proper and is therefore made FINAL.
Claims 28, 30-32, 42, 46, 49, 50, 54, 55 and 57 (non-elected inventions of Group II-VI, and non-elected species B) have been withdrawn from further considerations.
Claims 1, 2, 4, 5, 9, 11, 12, 14, 24 and 26 (elected invention of Group I with traverse; species A; directed to “An engineered formate dehydrogenase comprising a variant of amino acid sequence SEQ ID NO: 1…comprises a substitution at a residue corresponding to position 266 in SEQ ID NO: 1”), as currently amended, have been examined on their merits (to the extent they read on the elected species A) in this office action hereinafter.
Priority
This application is a 371 of PCT/US2022/075588 (filed on 08/29/2022), which
Claims domestic benefit from a US PRO 63/239,231 filed on 08/31/2021.
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.
1. Claims 1, 2, 4, 5, 9, 11, 12, 14, 24 and 26 (as currently recited) are 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 1 (as amended) is reproduced as follows:
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The recitation of limitations “wherein the engineered formate dehydrogenase comprises one or more alterations at a position described in TABLE 6…”, as currently presented in claim 1 renders the claimed scope of the product ambiguous and confusing, as it is not clear what exactly is being encompassed by the recitation as “described in Table 6” per se. See MPEP guidance below:
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Since, “one or more alterations at a position described in Table 6” as being incorporated into instant claim 1 would also encompass variety of parameters presented in Table 6, including presence and/or absence of comparative “activity” associated with specific type of variants and/or combinations thereof, the metes and bounds of the claimed product does not appear to be properly defined.
Since, none of the dependent claims clarify this point, they are also rejected as being indefinite for the same reason as discussed above. Appropriate correction is required.
2. Claim 4 recites the limitations, “wherein the engineered formate dehydrogenase comprises an activity that is at least 0.5, at least 1, at least 1.5, or at least 2-fold higher than the activity of a formate dehydrogenase consisting of the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 2”, wherein the limitations “the amino acid sequence of… SEQ ID NO: 2” lack proper antecedent basis in claim 1 (from which claim 4 directly depends from) as currently amended. In addition, the disclosure of “Table 6” (see SPEC, starting on p. 101) with specific variants of the “engineered formate dehydrogenase” do not appear to be compared to the activity of said enzyme “consisting of the amino acid sequences of” both SEQ ID NO: 1 and SEQ ID NO: 2, and therefore the recitation appears to be ambiguous and confusing.
Appropriate correction and/or explanation is required.
Claim Rejections - 35 USC § 112 - WD Requirement
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 1, 2, 4, 5, 9, 11, 12, 14, 24 and 26 (as amended/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.
Claim 1 recites the following:
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.
It is noted that regarding the limitations “functional fragment”, the instant disclosure states the following (see instant SPEC, p. 12-13, [0050]):
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However, other than the specific mutants/variants or amino acid substitutions/alterations disclosed in Table 6 pertaining to SEQ ID NO: 1, the disclosure of record does not provide guidance for any other “functional fragment”, for instance that have deletion(s) or truncations at ends of the enzyme protein as claimed, or for that matter any other type of “functional fragments” that have such truncations and/or alterations as currently encompassed by the product as claimed. As evidenced by the comparative activity profile disclosed in Table 6, provided by the applicants, it is clear that disclosure for such specific “functional” fragments (relevant to “some or all of the activity”) would require disclosure for core structure and/or variations for the enzyme protein alterations and details of such activity profile for such alterations, truncations, or deletions, etc., which is currently lacking on record. Thus, it is apparent that the subject matter as claimed has not been 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.
Appropriate correction and/or explanation 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 § 102
The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale, or otherwise available to the public before the effective filing date of the claimed invention.
Claims 1, 2, 4, 5, 9, 11, 12, 14, 24 and 26 (as amended/presented) are rejected under 35 U.S.C. 102(a)(1) as being anticipated by UniProt Accession No. A0A318DDF8 (2018; NPL cited in IDS dated 04/16/2026, citation C07; also published as NCBI ref. sequence with Accession No. WP_074551906.1, dated 10/06/2019; also attached as ref. [U] on PTO 892 form).
Claim 1 as currently amended is as follows;
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A0A318DDF8 (NCBI, 2018) discloses a formate dehydrogenase (having length of 386 amino acids) having 82 % identity and (89 % similarity) over 385 amino acid residues in a common overlap (range q:s: 1-385:1-385) with the instant sequence SEQ ID NO:1 (instant claim 1, as currently amended). The disclosed formate dehydrogenase comprises variants of amino acid sequence SEQ ID NO: 1, wherein the engineered formate dehydrogenase comprises one or more alterations at a position described as per TABLE 6, and wherein the one or more alterations comprises a substitution at a residue corresponding to position 266 (namely F266M, i.e. Phe to Met substitution; pertinent to instant claims 9 and 14) in SEQ ID NO: 1 (see homology shown below):
NCBI PROTEIN BLAST SEARCH (SEQ ID NO: 1):
NAD-dependent formate dehydrogenase [Dyella sp. AtDHG13]
Sequence ID: WP_074551906.1; Length: 386; Number of Matches: 1
Range 1: 1 to 385 GenPept Graphics Next Match Previous Match
Alignment statistics for match #1
Score
Expect
Method
Identities
Positives
Gaps
670 bits(1729)
0.0
Compositional matrix adjust.
315/385(82%)
345/385(89%)
0/385(0%)
Query 1 MSKILCVLYPDPVTGFPPVYARDSIPDIRCYPNGQTAPTPAGELGFTPGELVGSVSGELG 60
M+KI+CVLYPDPVTG+PP YARD +P I+ YPNGQT PTP GELGF PGEL+G VSGELG
Sbjct 1 MAKIVCVLYPDPVTGYPPAYARDDVPVIKGYPNGQTVPTPKGELGFKPGELIGCVSGELG 60
Query 61 LRRYLESQGHELIVTSDKEGADSVFERHLPDADVVISQPFWPAYLTAERIAKAKRLKLAL 120
LR+YLE+ GHELIVTSDKEG DSV +RHLP ADVVISQPFWPAYLTAERIAKAK LKLA+
Sbjct 61 LRKYLEANGHELIVTSDKEGVDSVLDRHLPTADVVISQPFWPAYLTAERIAKAKNLKLAI 120
Query 121 TAGIGSDHVDLKAAAERGITVAEVTFSNSISVAEHVVMTVLALVRNYLPAHQIANNGGWN 180
TAGIGSDHVDLKAA+E G+TVAEVTFSNSISVAEHV+MT L+LVRNYLP+HQIANNGGWN
Sbjct 121 TAGIGSDHVDLKAASEHGLTVAEVTFSNSISVAEHVMMTALSLVRNYLPSHQIANNGGWN 180
Query 181 IADCVARSYDVEGMHFGTLGAGRIGLAVLRRLKPFDMPLHYYDPHRLSAECEKELGLIYH 240
IADCV+RSYD+EGMHFGTL AGRIGLAVLRR+KPFD+ LHYYDPHRLS E EKEL +H
Sbjct 181 IADCVSRSYDIEGMHFGTLAAGRIGLAVLRRMKPFDVHLHYYDPHRLSPEIEKELNATFH 240
Query 241 DTPESLVSVCDVVNLQTPLYPATQGFVNAAFLAKFKRGAYLINTARGALCERDAIVHALE 300
+TPESL+ VCD+VNLQ PLYP+TQG + A KRGAYLINTARGALC+RDA+V ALE
Sbjct 241 ETPESLLKVCDIVNLQMPLYPSTQGMFDDKMFALMKRGAYLINTARGALCDRDAVVRALE 300
Query 301 TGQLAGYGGDVWFPQPAPIDHPWRRMPHQGMTPHISGTSLSGQARYAAGTLEILQNFLEG 360
+GQLAGYGGDVWFPQPAPIDHPWRRMPHQGMTPHISGTSLS QARYAAGTLEIL+ F E
Sbjct 301 SGQLAGYGGDVWFPQPAPIDHPWRRMPHQGMTPHISGTSLSAQARYAAGTLEILECFFEK 360
Query 361 KPIRQEYLIVDGGNLAGAGANAYKL 385
KPIR EYLIVDGGNLAG GA +YKL
Sbjct 361 KPIRPEYLIVDGGNLAGTGAASYKL 385
NAD-dependent formate dehydrogenase [Dyella sp. AtDHG13]
NCBI Reference Sequence: WP_074551906.1
LOCUS WP_074551906 386 aa linear BCT 06-OCT-2019
DEFINITION NAD-dependent formate dehydrogenase [Dyella sp. AtDHG13].
ACCESSION WP_074551906
VERSION WP_074551906.1
KEYWORDS RefSeq.
SOURCE Dyella sp. AtDHG13
ORGANISM Dyella sp. AtDHG13
Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
Lysobacterales; Rhodanobacteraceae; Dyella.
COMMENT REFSEQ: This record represents a single, non-redundant, protein
sequence which may be annotated on many different RefSeq genomes
from the same, or different, species.
##Evidence-For-Name-Assignment-START##
Evidence Category :: HMM
Evidence Accession :: NF005750.0
Evidence Source :: NCBI Protein Cluster (PRK)
Source Identifier :: PRK07574
##Evidence-For-Name-Assignment-END##
COMPLETENESS: full length.
FEATURES Location/Qualifiers
source 1..386
/organism="Dyella sp. AtDHG13"
/db_xref="taxon:1938897"
Protein 1..386
/product="NAD-dependent formate dehydrogenase"
/GO_function="GO:0008863 - formate dehydrogenase (NAD+)
activity [Evidence IEA]; GO:0051287 - NAD binding
[Evidence IEA]"
/calculated_mol_wt=42008
Region 1..386
/region_name="PRK07574"
/note="NAD-dependent formate dehydrogenase"
/db_xref="CDD:181041"
ORIGIN
1 makivcvlyp dpvtgyppay arddvpvikg ypngqtvptp kgelgfkpge ligcvsgelg
61 lrkyleangh elivtsdkeg vdsvldrhlp tadvvisqpf wpayltaeri akaknlklai
121 tagigsdhvd lkaasehglt vaevtfsnsi svaehvmmta lslvrnylps hqiannggwn
181 iadcvsrsyd iegmhfgtla agriglavlr rmkpfdvhlh yydphrlspe iekelnatfh
241 etpesllkvc divnlqmply pstqgmfddk mfalmkrgay lintargalc drdavvrale
301 sgqlagyggd vwfpqpapid hpwrrmphqg mtphisgtsl saqaryaagt leilecffek
361 kpirpeyliv dggnlagtga asyklt
//
It is noted that the engineered formate dehydrogenase of A0A318DDF8 is capable of conversions a) to c) as recited in instant claim 2, and comprises at least amino acid alterations at positions 2, 16, 19, 27, 29, 30, 41, 120, 191, 217, 218, 231, 238, 262, 267, 269, 271, 291, 297, 301, 342, 355, 365, 381, 382 (as per instant disclosure in TABLE 6; pertinent to instant claim 5). Since, the same variant as recited in instant claim 1 has been disclosed by the cited prior art reference, the activity as required by instant claim 4 would be taken to be the same, unless evidence/data provided on record to the contrary; wherein (regarding instant claims 11-12) the one or more amino acid alterations are conservative amino acid substitutions, as well as non-conservative amino acid substitutions (for instance, F266M taken as “conservative” substitution; A269D taken as “non-conservative” substitution; see applicant’s disclosure at p. 10, [0044] for such terms). In addition, applicant’s SEQ ID NO: 24 consists of the following amino acid sequence:
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It is clear from the above disclosure that the amino acid sequence disclosed by the cited prior art A0A318DDF8 (or WP_074551906.1) does not consist of the amino acid sequence of SEQ ID NO: 24 (a 364 amino acid variant), as provided by applicants.
Thus, the limitations of instant claims 1, 2, 4, 5, 9, 11, 12, 14, 24 and 26, as currently presented, are deemed to be anticipated by the disclosure from the cited prior art reference, as discussed above.
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
ADDITIONAL PERTINENT SEARCH RESULTS (SEQ ID NO: 1, Claim 1):
UNIPROT DATABASE RESULTS:
RESULT 13
A0A0M3AKF0_9SPHN
ID A0A0M3AKF0_9SPHN Unreviewed; 386 AA.
AC A0A0M3AKF0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 08-OCT-2025, entry version 42.
DE RecName: Full=Formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128, ECO:0000256|HAMAP-Rule:MF_03210};
DE Short=FDH {ECO:0000256|HAMAP-Rule:MF_03210};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128, ECO:0000256|HAMAP-Rule:MF_03210};
DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03210};
GN ORFNames=YP76_20875 {ECO:0000313|EMBL:KKW90438.1};
OS Sphingobium chungbukense.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Sphingomonadales; Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=56193 {ECO:0000313|EMBL:KKW90438.1, ECO:0000313|Proteomes:UP000033874};
RN [1] {ECO:0000313|EMBL:KKW90438.1, ECO:0000313|Proteomes:UP000033874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ77 {ECO:0000313|EMBL:KKW90438.1,
RC ECO:0000313|Proteomes:UP000033874};
RA Kim Y.-C., Chae J.-C.;
RT "Genome sequence of aromatic hydrocarbons-degrading Sphingobium
RT chungbukense DJ77.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon
CC dioxide. Formate oxidation is the final step in the methanol oxidation
CC pathway in methylotrophic microorganisms. Has a role in the
CC detoxification of exogenous formate in non-methylotrophic organisms.
CC {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455, ECO:0000256|HAMAP-
CC Rule:MF_03210};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. FDH subfamily. {ECO:0000256|HAMAP-Rule:MF_03210}.
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:KKW90438.1}.
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DR EMBL; LBIC01000010; KKW90438.1; -; Genomic_DNA.
DR RefSeq; WP_046765524.1; NZ_LBIC01000010.1.
DR AlphaFoldDB; A0A0M3AKF0; -.
DR STRING; 56193.YP76_20875; -.
DR PATRIC; fig|56193.3.peg.4384; -.
DR Proteomes; UP000033874; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0042183; P:formate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05302; FDH; 1.
DR FunFam; 3.40.50.720:FF:000057; Formate dehydrogenase; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_03210; Formate_dehydrogenase; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR033689; FDH_NAD-dep.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF005750; PRK07574.1; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03210};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03210}; Reference proteome {ECO:0000313|Proteomes:UP000033874}.
FT DOMAIN 65..364
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 157..336
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 203..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 258..262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 334..337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 286
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 334
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ SEQUENCE 386 AA; 42223 MW; F083C9825EDCCDFA CRC64;
Query Match 81.9%; Score 1663; Length 386;
Best Local Similarity 80.3%;
Matches 309; Conservative 30; Mismatches 46; Indels 0; Gaps 0;
Qy 1 MSKILCVLYPDPVTGFPPVYARDSIPDIRCYPNGQTAPTPAGELGFTPGELVGSVSGELG 60
|:|:|||||||| ||:|| |||| :| | |||||| ||| ||||| |||||| ||||||
Db 1 MAKVLCVLYPDPTTGYPPKYARDDLPVINSYPNGQTLPTPRGELGFKPGELVGCVSGELG 60
Qy 61 LRRYLESQGHELIVTSDKEGADSVFERHLPDADVVISQPFWPAYLTAERIAKAKRLKLAL 120
|| :||: || |::|||||| :| |:||| |||||||||||||||| |||||||:|||||
Db 61 LRPWLEANGHTLVITSDKEGPNSEFDRHLVDADVVISQPFWPAYLTPERIAKAKKLKLAL 120
Qy 121 TAGIGSDHVDLKAAAERGITVAEVTFSNSISVAEHVVMTVLALVRNYLPAHQIANNGGWN 180
|||||||||||||||| |||||| |||||||||||||| ||:|||||||:|:|| ||||
Db 121 TAGIGSDHVDLKAAAEHGITVAEETFSNSISVAEHVVMMVLSLVRNYLPSHEIAREGGWN 180
Qy 181 IADCVARSYDVEGMHFGTLGAGRIGLAVLRRLKPFDMPLHYYDPHRLSAECEKELGLIYH 240
|||||||||||||| |||| ||||||||||||||||: |||||||||||: | |||| ||
Db 181 IADCVARSYDVEGMQFGTLAAGRIGLAVLRRLKPFDVKLHYYDPHRLSADLEAELGLTYH 240
Qy 241 DTPESLVSVCDVVNLQTPLYPATQGFVNAAFLAKFKRGAYLINTARGALCERDAIVHALE 300
|||:||: |||:|||| ||||:||| | |: |||||||||||||||:|||:| |||
Db 241 DTPQSLIKVCDIVNLQMPLYPSTQGMFNDEMFAQMKRGAYLINTARGALCDRDAVVRALE 300
Qy 301 TGQLAGYGGDVWFPQPAPIDHPWRRMPHQGMTPHISGTSLSGQARYAAGTLEILQNFLEG 360
:|||||| |||||||||| ||||| ||: ||||||||:||| |||||||||||||:| ||
Db 301 SGQLAGYAGDVWFPQPAPADHPWRTMPNNGMTPHISGSSLSAQARYAAGTLEILQDFFEG 360
Qy 361 KPIRQEYLIVDGGNLAGAGANAYKL 385
:|||:|||||| ||||| |||:|||
Db 361 RPIRREYLIVDAGNLAGTGANSYKL 385
RESULT 15
A0A1N6IVW6_9BURK
ID A0A1N6IVW6_9BURK Unreviewed; 386 AA.
AC A0A1N6IVW6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 30.
DE RecName: Full=Formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128, ECO:0000256|HAMAP-Rule:MF_03210};
DE Short=FDH {ECO:0000256|HAMAP-Rule:MF_03210};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128, ECO:0000256|HAMAP-Rule:MF_03210};
DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03210};
GN ORFNames=SAMN05444165_2535 {ECO:0000313|EMBL:SIO36046.1};
OS Paraburkholderia phenazinium.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=60549 {ECO:0000313|EMBL:SIO36046.1, ECO:0000313|Proteomes:UP000185151};
RN [1] {ECO:0000313|EMBL:SIO36046.1, ECO:0000313|Proteomes:UP000185151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS95 {ECO:0000313|EMBL:SIO36046.1,
RC ECO:0000313|Proteomes:UP000185151};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon
CC dioxide. Formate oxidation is the final step in the methanol oxidation
CC pathway in methylotrophic microorganisms. Has a role in the
CC detoxification of exogenous formate in non-methylotrophic organisms.
CC {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455, ECO:0000256|HAMAP-
CC Rule:MF_03210};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. FDH subfamily. {ECO:0000256|HAMAP-Rule:MF_03210}.
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DR EMBL; FSRU01000001; SIO36046.1; -; Genomic_DNA.
DR RefSeq; WP_074295970.1; NZ_FSRU01000001.1.
DR AlphaFoldDB; A0A1N6IVW6; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000185151; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0042183; P:formate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05302; FDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_03210; Formate_dehydrogenase; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR033689; FDH_NAD-dep.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF005750; PRK07574.1; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03210};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03210}; Reference proteome {ECO:0000313|Proteomes:UP000185151}.
FT DOMAIN 63..362
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 157..336
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 203..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 258..262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 334..337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 286
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 334
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ SEQUENCE 386 AA; 42229 MW; 5566562675A6B173 CRC64;
Query Match 81.7%; Score 1659; Length 386; Best Local Similarity 80.0%;
Matches 308; Conservative 32; Mismatches 45; Indels 0; Gaps 0;
Qy 1 MSKILCVLYPDPVTGFPPVYARDSIPDIRCYPNGQTAPTPAGELGFTPGELVGSVSGELG 60
|:|:|||||||||||:|| |||: || | |||||| |:| | ||| |||||| ||||||
Db 1 MAKVLCVLYPDPVTGYPPKYARNEIPVITAYPNGQTVPSPKGPLGFKPGELVGCVSGELG 60
Qy 61 LRRYLESQGHELIVTSDKEGADSVFERHLPDADVVISQPFWPAYLTAERIAKAKRLKLAL 120
||||||| ||||:|||||:|||| |:||||||||||||||||||||||||||||:|||||
Db 61 LRRYLESHGHELVVTSDKDGADSTFDRHLPDADVVISQPFWPAYLTAERIAKAKKLKLAL 120
Qy 121 TAGIGSDHVDLKAAAERGITVAEVTFSNSISVAEHVVMTVLALVRNYLPAHQIANNGGWN 180
||||||||||||||| |||||| |||||||||||||| ||:|||||||:|| | |||||
Db 121 TAGIGSDHVDLKAAAAHGITVAEETFSNSISVAEHVVMMVLSLVRNYLPSHQYAVNGGWN 180
Qy 181 IADCVARSYDVEGMHFGTLGAGRIGLAVLRRLKPFDMPLHYYDPHRLSAECEKELGLIYH 240
|||||:||||:|||||||: ||||||||||||||||: |||||||||||| |:|| | ||
Db 181 IADCVSRSYDLEGMHFGTIAAGRIGLAVLRRLKPFDVHLHYYDPHRLSAEIERELNLTYH 240
Qy 241 DTPESLVSVCDVVNLQTPLYPATQGFVNAAFLAKFKRGAYLINTARGALCERDAIVHALE 300
|||||| ||||:|||:||||||: : | | |||||||| ||:|||:| |||
Db 241 PTPESLVKVCDVINLQSPLYPATEHMFDDRMFELVKHGTYLINTARGKLCDRDAVVRALE 300
Qy 301 TGQLAGYGGDVWFPQPAPIDHPWRRMPHQGMTPHISGTSLSGQARYAAGTLEILQNFLEG 360
:|:|||| ||||:|||||:||||||||:|||||||||:||:|||||||||||||: | ||
Db 301 SGKLAGYAGDVWYPQPAPVDHPWRRMPNQGMTPHISGSSLAGQARYAAGTLEILECFFEG 360
Qy 361 KPIRQEYLIVDGGNLAGAGANAYKL 385
:||| |||||||||||| || :|||
Db 361 RPIRPEYLIVDGGNLAGTGAGSYKL 385
RESULT 16
A0A1H7HQD2_9BURK
ID A0A1H7HQD2_9BURK Unreviewed; 386 AA.
AC A0A1H7HQD2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=Formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128, ECO:0000256|HAMAP-Rule:MF_03210};
DE Short=FDH {ECO:0000256|HAMAP-Rule:MF_03210};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128, ECO:0000256|HAMAP-Rule:MF_03210};
DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_03210};
GN ORFNames=SAMN05192542_102306 {ECO:0000313|EMBL:SEK50435.1};
OS Paraburkholderia caballeronis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416943 {ECO:0000313|EMBL:SEK50435.1, ECO:0000313|Proteomes:UP000199120};
RN [1] {ECO:0000313|Proteomes:UP000199120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26416 {ECO:0000313|Proteomes:UP000199120};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of formate to carbon
CC dioxide. Formate oxidation is the final step in the methanol oxidation
CC pathway in methylotrophic microorganisms. Has a role in the
CC detoxification of exogenous formate in non-methylotrophic organisms.
CC {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00000455, ECO:0000256|HAMAP-
CC Rule:MF_03210};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. FDH subfamily. {ECO:0000256|HAMAP-Rule:MF_03210}.
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CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOAJ01000002; SEK50435.1; -; Genomic_DNA.
DR RefSeq; WP_090540981.1; NZ_FNSR01000001.1.
DR AlphaFoldDB; A0A1H7HQD2; -.
DR STRING; 416943.SAMN05445871_0003; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000199120; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0042183; P:formate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd05302; FDH; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR HAMAP; MF_03210; Formate_dehydrogenase; 1.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR033689; FDH_NAD-dep.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF005750; PRK07574.1; 1.
DR PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03210};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_03210};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03210}; Reference proteome {ECO:0000313|Proteomes:UP000199120}.
FT DOMAIN 63..362
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 157..336
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 203..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 223
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 258..262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 284
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 334..337
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 382
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 286
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 334
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ SEQUENCE 386 AA; 42536 MW; B51E8ACAFC5AA3AC CRC64;
Query Match 81.4%; Score 1654; Length 386; Best Local Similarity 79.2%;
Matches 305; Conservative 34; Mismatches 46; Indels 0; Gaps 0;
Qy 1 MSKILCVLYPDPVTGFPPVYARDSIPDIRCYPNGQTAPTPAGELGFTPGELVGSVSGELG 60
|:|:|||||||||||:|| |||| || |: |||||| |:| ||||| ||:||| ||||||
Db 1 MAKVLCVLYPDPVTGYPPKYARDDIPVIKGYPNGQTVPSPEGELGFKPGDLVGCVSGELG 60
Qy 61 LRRYLESQGHELIVTSDKEGADSVFERHLPDADVVISQPFWPAYLTAERIAKAKRLKLAL 120
||:|||| ||||:||||||| || |||||||||:|||||||||||| |||||||:|||||
Db 61 LRKYLESHGHELVVTSDKEGVDSTFERHLPDADIVISQPFWPAYLTPERIAKAKKLKLAL 120
Qy 121 TAGIGSDHVDLKAAAERGITVAEVTFSNSISVAEHVVMTVLALVRNYLPAHQIANNGGWN 180
||||||||||||||| ||:||||||||||||||||||| |:|||||||:|| | |||||
Db 121 TAGIGSDHVDLKAAAARGVTVAEVTFSNSISVAEHVVMMTLSLVRNYLPSHQFAVNGGWN 180
Qy 181 IADCVARSYDVEGMHFGTLGAGRIGLAVLRRLKPFDMPLHYYDPHRLSAECEKELGLIYH 240
||||| ||||:|||||||: ||||||||||||||||: |||||||||| : | || | ||
Db 181 IADCVTRSYDLEGMHFGTIAAGRIGLAVLRRLKPFDVHLHYYDPHRLSPQIEAELNLTYH 240
Qy 241 DTPESLVSVCDVVNLQTPLYPATQGFVNAAFLAKFKRGAYLINTARGALCERDAIVHALE 300
:||:||| ||||:||||||||:|: : |||||||||||| ||:|||:| |:|
Db 241 ETPQSLVKVCDVINLQTPLYPSTEHMFDDRMFELVKRGAYLINTARGKLCDRDAVVRAVE 300
Qy 301 TGQLAGYGGDVWFPQPAPIDHPWRRMPHQGMTPHISGTSLSGQARYAAGTLEILQNFLEG 360
:|:|||| ||||:|||||:||||||||::|||||||||||| | ||||||||||| ||:
Db 301 SGRLAGYAGDVWYPQPAPVDHPWRRMPYEGMTPHISGTSLSAQHRYAAGTLEILQCFLDR 360
Qy 361 KPIRQEYLIVDGGNLAGAGANAYKL 385
|||| |||||||||||| || :|||
Db 361 KPIRPEYLIVDGGNLAGTGAGSYKL 385
Prosecution Insights