FDH1_YEAST
ID FDH1_YEAST Reviewed; 376 AA.
AC Q08911; D6W381;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Formate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|PubMed:9178506};
DE Short=FDH {ECO:0000255|HAMAP-Rule:MF_03210};
DE EC=1.17.1.9 {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:12144528};
DE AltName: Full=NAD-dependent formate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000303|PubMed:11921099};
GN Name=FDH1 {ECO:0000303|PubMed:9178506};
GN OrderedLocusNames=YOR388C {ECO:0000312|SGD:S000005915};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION.
RX PubMed=9178506;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<551::aid-yea113>3.0.co;2-0;
RA van den Berg M.A., Steensma H.Y.;
RT "Expression cassettes for formaldehyde and fluoroacetate resistance, two
RT dominant markers in Saccharomyces cerevisiae.";
RL Yeast 13:551-559(1997).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF 197-ASP-TYR-198.
RX PubMed=12144528; DOI=10.1042/bj20020379;
RA Serov A.E., Popova A.S., Fedorchuk V.V., Tishkov V.I.;
RT "Engineering of coenzyme specificity of formate dehydrogenase from
RT Saccharomyces cerevisiae.";
RL Biochem. J. 367:841-847(2002).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
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 (PubMed:9178506,
CC PubMed:12144528, PubMed:11921099). Has a role in the detoxification of
CC exogenous formate in non-methylotrophic organisms (PubMed:11921099).
CC {ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:11921099,
CC ECO:0000269|PubMed:12144528, ECO:0000269|PubMed:9178506}.
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, ECO:0000269|PubMed:12144528};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.5 mM for formate {ECO:0000269|PubMed:12144528};
CC KM=36 uM for NAD(+) {ECO:0000269|PubMed:12144528};
CC Note=kcat is 6.5 sec(-1) with NAD(+) as substrate.
CC {ECO:0000269|PubMed:9178506};
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; Z75296; CAA99720.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11147.1; -; Genomic_DNA.
DR PIR; S67300; S67300.
DR RefSeq; NP_015033.1; NM_001183808.1.
DR AlphaFoldDB; Q08911; -.
DR SMR; Q08911; -.
DR BioGRID; 34769; 81.
DR DIP; DIP-5327N; -.
DR IntAct; Q08911; 4.
DR MINT; Q08911; -.
DR STRING; 4932.YOR388C; -.
DR PaxDb; Q08911; -.
DR PRIDE; Q08911; -.
DR EnsemblFungi; YOR388C_mRNA; YOR388C; YOR388C.
DR GeneID; 854570; -.
DR KEGG; sce:YOR388C; -.
DR SGD; S000005915; FDH1.
DR VEuPathDB; FungiDB:YOR388C; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_0_0_1; -.
DR InParanoid; Q08911; -.
DR OMA; HYTDRHR; -.
DR BioCyc; YEAST:YOR388C-MON; -.
DR BRENDA; 1.17.1.9; 984.
DR PRO; PR:Q08911; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08911; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IDA:SGD.
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; IGI:SGD.
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 1: Evidence at protein level;
KW Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..376
FT /note="Formate dehydrogenase 1"
FT /id="PRO_0000223647"
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"
FT MUTAGEN 197..198
FT /note="DY->AR: Shifts the coenzyme preference of the enzyme
FT from NAD(+) to NADP(+)."
FT /evidence="ECO:0000269|PubMed:12144528"
SQ SEQUENCE 376 AA; 41714 MW; 67ECDA6F9DDC2A02 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 LDAQKRYAQG VKNILNSYFS KKFDYRPQDI
IVQNGSYATR AYGQKK
