ID   FDH_PICAN               Reviewed;         362 AA.
AC   P33677;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   10-JUN-2026, entry version 102.
DE   RecName: Full=Formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|Ref.1};
DE            Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210};
DE            EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210};
DE   AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210};
GN   Name=FMDH {ECO:0000303|Ref.1};
OS   Pichia angusta (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC   Pichiales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=870730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC   Y-5445;
RA   Hollenberg C.P., Janowicz Z.;
RT   "DNA-molecules coding for FMDH control regions and structured gene for a
RT   protein having FMDH-activity and their uses.";
RL   Patent number EP0299108, 18-JAN-1989.
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_03210};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_03210}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03210}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-Rule:MF_03210}.
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DR   EMBL; A06214; CAA00531.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P33677; -.
DR   SMR; P33677; -.
DR   BRENDA; 1.17.1.9; 2587.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; 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; 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   NCBIfam; NF005750; PRK07574.1; 1.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 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; NAD; Oxidoreductase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..362
FT                   /note="Formate dehydrogenase"
FT                   /id="PRO_0000076025"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         174..175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         230..234
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         256
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         282
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         311..314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   BINDING         357
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   SITE            258
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT   SITE            311
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
SQ   SEQUENCE   362 AA;  39911 MW;  0037BFD132FC055B CRC64;
     MKVVLVLYDA GKHAQDEERL YGCTENALGI RDWLEKQGHD VVVTSDKEGQ NSVLEKNISD
     ADVIISTPFH PAYITKERID KAKKLKLLVV AGVGSDHIDL DYINQSGRDI SVLEVTGSNV
     VSVAEHVVMT MLVLVRNFVP AHEQIISGGW NVAEIAKDSF DIEGKVIATI GAGRIGYRVL
     ERLVAFNPKE LLYYDYQSLS KEAEEKVGAR RVHDIKELVA QADIVTINCP LHAGSKGLVN
     AELLKHFKKG AWLVNTARGA ICVAEDVAAA VKSGQLRGYG GDVWFPQPAP KDHPWRSMAN
     KYGAGNAMTP HYSGSVIDAQ VRYAQGTKNI LESFFTQKFD YRPQDIILLN GKYKTKSYGA
     DK
//