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Database: UniProt
Entry: A0A0M9VTN4_9HYPO
LinkDB: A0A0M9VTN4_9HYPO
Original site: A0A0M9VTN4_9HYPO 
ID   A0A0M9VTN4_9HYPO        Unreviewed;       367 AA.
AC   A0A0M9VTN4;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=ESCO_000670 {ECO:0000313|EMBL:KOS18855.1};
OS   Escovopsis weberi.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Escovopsis.
OX   NCBI_TaxID=150374 {ECO:0000313|EMBL:KOS18855.1, ECO:0000313|Proteomes:UP000053831};
RN   [1] {ECO:0000313|EMBL:KOS18855.1, ECO:0000313|Proteomes:UP000053831}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   de Man T.J., Stajich J.E., Kubicek C.P., Chenthamara K., Atanasova L.,
RA   Druzhinina I.S., Birnbaum S., Barribeau S.M., Teiling C., Suen G.,
RA   Currie C., Gerardo N.M.;
RT   "The genome of the fungus Escovopsis weberi, a specialized disease agent of
RT   ant agriculture.";
RL   Submitted (JUL-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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:KOS18855.1}.
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DR   EMBL; LGSR01000020; KOS18855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9VTN4; -.
DR   STRING; 150374.A0A0M9VTN4; -.
DR   OrthoDB; 946665at2759; -.
DR   Proteomes; UP000053831; 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; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR033689; FDH_NAD-dep.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 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|HAMAP-Rule:MF_03210};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_03210,
KW   ECO:0000256|RuleBase:RU003719};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053831}.
FT   DOMAIN          38..343
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT                   catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00389"
FT   DOMAIN          135..318
FT                   /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02826"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   BINDING         125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   BINDING         180..181
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   BINDING         201
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   BINDING         236..240
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   BINDING         262
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   BINDING         288
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   BINDING         317..320
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   BINDING         363
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   SITE            264
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT   SITE            317
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ   SEQUENCE   367 AA;  40679 MW;  964D6A4735C345A6 CRC64;
     MVFLRPVKVL LVLYDGHEHA EQVPELLGTT ENELGLRKWL EEQGHELVTT SDKDRENSKF
     DQELVDAEVI ITTPFHPGYL TAERLAKAKK LKIAITAGIG SDHVDLNAAN VTNGGITVAE
     VTGSNVVSVA EHVVMTILVL LRNFVPAHEQ VERGDWNVAQ VAKQSFDLEG KVVGTVAVGR
     IGERVLRRLK PFDCKELLYY DYQPLSAEKE AEIGCRRVES LEEMLAQCDV VTINCPLHEK
     TKGLFNKELI SKMKKGSYLV NTARGAIVVK EDVAEALKSG HLAGYGGDVW FPQPAPSDHC
     LRTAKNPFGF GNAMVPHMSG TTLDAQKRYA DGTKAILESY FSGRHDYRPQ DLIVYKGDYA
     TRSYGQR
//
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