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Database: UniProt
Entry: Q08911
LinkDB: Q08911
Original site: Q08911 
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   13-FEB-2019, entry version 132.
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;
OC   Saccharomycetes; 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.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   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.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   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,
RT   two 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
CC       carbon dioxide. Formate oxidation is the final step in the
CC       methanol oxidation pathway in methylotrophic microorganisms
CC       (PubMed:9178506, PubMed:12144528, PubMed:11921099). Has a role in
CC       the detoxification of exogenous formate in non-methylotrophic
CC       organisms (PubMed:11921099). {ECO:0000255|HAMAP-Rule:MF_03210,
CC       ECO:0000269|PubMed:11921099, ECO:0000269|PubMed:12144528,
CC       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-
CC       Rule:MF_03210}.
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   ProteinModelPortal; Q08911; -.
DR   SMR; Q08911; -.
DR   BioGrid; 34769; 79.
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_mRNA; YOR388C.
DR   GeneID; 854570; -.
DR   KEGG; sce:YOR388C; -.
DR   EuPathDB; FungiDB:YOR388C; -.
DR   SGD; S000005915; FDH1.
DR   HOGENOM; HOG000136703; -.
DR   InParanoid; Q08911; -.
DR   KO; K00122; -.
DR   OMA; EVTYCNS; -.
DR   BioCyc; YEAST:YOR388C-MONOMER; -.
DR   BRENDA; 1.2.1.2; 984.
DR   PRO; PR:Q08911; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
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   Complete proteome; Cytoplasm; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    376       Formate dehydrogenase 1.
FT                                /FTId=PRO_0000223647.
FT   NP_BIND     176    177       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     244    248       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   NP_BIND     325    328       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   REGION        5    121       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      122    326       Coenzyme-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   REGION      327    372       Catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING      97     97       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     121    121       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_03210}.
FT   BINDING     197    197       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     270    270       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   BINDING     296    296       NAD. {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        272    272       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   SITE        325    325       Important for catalytic activity.
FT                                {ECO:0000255|HAMAP-Rule:MF_03210}.
FT   MUTAGEN     197    198       DY->AR: Shifts the coenzyme preference of
FT                                the enzyme from NAD(+) to NADP(+).
FT                                {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
//
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