ID A2R4H2_ASPNC Unreviewed; 360 AA.
AC A2R4H2;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 96.
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=An15g00410 {ECO:0000313|EMBL:CAK42210.1};
OS Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK42210.1, ECO:0000313|Proteomes:UP000006706};
RN [1] {ECO:0000313|EMBL:CAK42210.1, ECO:0000313|Proteomes:UP000006706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC {ECO:0000313|Proteomes:UP000006706};
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA van Ooyen A.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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}.
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DR EMBL; AM270330; CAK42210.1; -; Genomic_DNA.
DR RefSeq; XP_001396580.2; XM_001396543.2.
DR AlphaFoldDB; A2R4H2; -.
DR EnsemblFungi; CAK42210; CAK42210; An15g00410.
DR GeneID; 4987640; -.
DR HOGENOM; CLU_019796_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 3R.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03210}; Reference proteome {ECO:0000313|Proteomes:UP000006706}.
FT DOMAIN 30..124
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 125..295
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 170..171
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 226..230
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 307..310
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 254
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 307
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ SEQUENCE 360 AA; 39510 MW; DD9E1744217F27CE CRC64;
MVLYDGGEHA KQQPGLLGTT ENELGLRKWL EEQGHTLVTT SDKEGENSTF DKELVDAEVI
ITTPFHPGYL TAERLAKAKN LKIAVTAGVG SDHVDLNAAN KTNGGITVAE VTGCNVVSVA
EHVVMTILTL VRNFVPAHEQ IRRGEWDVAA VAKNEFDLEG KVVGTVAVGR IGERVLRRLK
PFDCKELLYY DYQPLAPEVE KEIGCRRVDN LEEMLAQCDV VTINCPLHEK TRGLFNKELI
SKMKKGSWLV NTARGAIVVK EDVAEAVKSG HLRGYGGDVW FPQPAPADHP LRTVQGPWGG
GNAMVPHMSG TSIDAQIRYA NGTKAILESY FSGRHDYRPE DLIVHGGDYV TKAYGQRNKA
//
