ID A0A369JUK2_HYPMA Unreviewed; 420 AA.
AC A0A369JUK2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=aciA {ECO:0000313|EMBL:RDB24890.1};
GN ORFNames=Hypma_007750 {ECO:0000313|EMBL:RDB24890.1};
OS Hypsizygus marmoreus (White beech mushroom) (Agaricus marmoreus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Hypsizygus.
OX NCBI_TaxID=39966 {ECO:0000313|EMBL:RDB24890.1, ECO:0000313|Proteomes:UP000076154};
RN [1] {ECO:0000313|EMBL:RDB24890.1, ECO:0000313|Proteomes:UP000076154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=51987-8 {ECO:0000313|EMBL:RDB24890.1,
RC ECO:0000313|Proteomes:UP000076154};
RA Choi I.-G., Min B., Kim J.-G., Kim S., Oh Y.-L., Kong W.-S., Park H.,
RA Jeong J., Song E.-S.;
RT "Whole genome sequencing of Hypsizygus marmoreus.";
RL Submitted (APR-2018) 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:RDB24890.1}.
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DR EMBL; LUEZ02000041; RDB24890.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369JUK2; -.
DR STRING; 39966.A0A369JUK2; -.
DR InParanoid; A0A369JUK2; -.
DR Proteomes; UP000076154; 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|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_03210}; Reference proteome {ECO:0000313|Proteomes:UP000076154}.
FT DOMAIN 93..399
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 189..360
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 234..235
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 255
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 290..294
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 342
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT BINDING 371..374
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 318
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
FT SITE 371
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03210"
SQ SEQUENCE 420 AA; 46202 MW; A095953F1027DA46 CRC64;
MIPHTTPLFG PSVRSAERNG KLTGHREESS LGCRDNHLTL GEYRILWCAF SQQFTMKVLA
ILYNGFKAAE EEPRLLGTVE NQLGIQEWLT SQGHELIGKR GFPLVSSSKE GPDSDFQKHI
VDAEVLITTP FHPGYLTRDL IEKAKNLKIC ITAGVGSDHI DLNAAVDNKI QVLEVSGSNV
VSVAEHVIMS ILLLVRNFVP AHEMIERGDW QVSDIARNAF DLEGKVVGTI GAGRIGYRVL
QRLVPFDCKE LLYYDYAPLP AEAAKAVKVR RVEDLKDFVS QCDVVTVNCP LHEGTRGLVN
AELLKHFKKG AWLVNTARGA ICDKDAVAEA LKSGQLSGYS GDVWNVQPAP KDHIWRTMKN
PLGGGNGMVP HYSGTTLDAQ ARYANGTKSI LSNYLEGKPQ EPQNIIVGLG KYETSAYGQR
//
