FDH2_YEASC
ID FDH2_YEASC Reviewed; 376 AA.
AC P0CT22;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 1.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Formate dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_03210};
DE Short=FDH 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_03210};
GN Name=FDH2;
OS Saccharomyces cerevisiae (strain CEN.PK113-7D) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=889517;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEN.PK113-7D;
RX PubMed=22448915; DOI=10.1186/1475-2859-11-36;
RA Nijkamp J.F., van den Broek M., Datema E., de Kok S., Bosman L.,
RA Luttik M.A., Daran-Lapujade P., Vongsangnak W., Nielsen J., Heijne W.H.M.,
RA Klaassen P., Paddon C.J., Platt D., Koetter P., van Ham R.C.,
RA Reinders M.J.T., Pronk J.T., de Ridder D., Daran J.-M.;
RT "De novo sequencing, assembly and analysis of the genome of the laboratory
RT strain Saccharomyces cerevisiae CEN.PK113-7D, a model for modern industrial
RT biotechnology.";
RL Microb. Cell Fact. 11:36-36(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-204, FUNCTION, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RC STRAIN=CEN.PK113-7D;
RX PubMed=11921099; DOI=10.1002/yea.856;
RA Overkamp K.M., Koetter P., van der Hoek R., Schoondermark-Stolk S.,
RA Luttik M.A.H., van Dijken J.P., Pronk J.T.;
RT "Functional analysis of structural genes for NAD(+)-dependent formate
RT dehydrogenase in Saccharomyces cerevisiae.";
RL Yeast 19:509-520(2002).
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 ECO:0000269|PubMed:11921099}.
CC -!- INDUCTION: Induced by formate. {ECO:0000269|PubMed:11921099}.
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; CM001537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P0CT22; -.
DR SMR; P0CT22; -.
DR Proteomes; UP000013192; Chromosome XVI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC.
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 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 Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; NAD; Oxidoreductase.
FT CHAIN 1..376
FT /note="Formate dehydrogenase 2"
FT /id="PRO_0000423513"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 176..177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 197
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 244..248
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT BINDING 325..328
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT SITE 272
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
FT SITE 325
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03210"
SQ SEQUENCE 376 AA; 41736 MW; 67ECDA6F921316FE CRC64;
MSKGKVLLVL YEGGKHAEEQ EKLLGCIENE LGIRNFIEEQ GYELVTTIDK DPEPTSTVDR
ELKDAEIVIT TPFFPAYISR NRIAEAPNLK LCVTAGVGSD HVDLEAANER KITVTEVTGS
NVVSVAEHVM ATILVLIRNY NGGHQQAING EWDIAGVAKN EYDLEDKIIS TVGAGRIGYR
VLERLVAFNP KKLLYYDYQE LPAEAINRLN EASKLFNGRG DIVQRVEKLE DMVAQSDVVT
INCPLHKDSR GLFNKKLISH MKDGAYLVNT ARGAICVAED VAEAVKSGKL AGYGGDVWDK
QPAPKDHPWR TMDNKDHVGN AMTVHISGTS LHAQKRYAQG VKNILNSYFS KKFDYRPQDI
IVQNGSYATR AYGQKK
