ID   FDH1_YEAST              Reviewed;         376 AA.
AC   Q08911;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 58.
DE   RecName: Full=Formate dehydrogenase 1;
DE            EC=1.2.1.2;
DE   AltName: Full=NAD-dependent formate dehydrogenase 1;
GN   Name=FDH1; OrderedLocusNames=YOR388C;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   MEDLINE=97313270; 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   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   [3]
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   -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Induced by formate.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily.
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DR   EMBL; Z75296; CAA99720.1; -; Genomic_DNA.
DR   PIR; S67300; S67300.
DR   RefSeq; NP_015033.1; -.
DR   HSSP; P33160; 2NAD.
DR   DIP; DIP:5327N; -.
DR   IntAct; Q08911; 5.
DR   Ensembl; YOR388C; Saccharomyces cerevisiae.
DR   GeneID; 854570; -.
DR   GenomeReviews; Y13140_GR; YOR388C.
DR   KEGG; sce:YOR388C; -.
DR   NMPDR; fig|4932.3.peg.6154; -.
DR   CYGD; YOR388c; -.
DR   SGD; S000005915; FDH1.
DR   HOGENOM; Q08911; -.
DR   OMA; Q08911; FHPAYIT.
DR   BRENDA; 1.2.1.2; 250.
DR   NextBio; 977021; -.
DR   GermOnline; YOR388C; Saccharomyces cerevisiae.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0008863; F:formate dehydrogenase activity; IGI:SGD.
DR   GO; GO:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-O...; IEA:InterPro.
DR   GO; GO:0042183; P:formate catabolic process; IGI:SGD.
DR   GO; GO:0006735; P:NADH regeneration; TAS:SGD.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH.
DR   InterPro; IPR006140; D-isomer_2_OHA_DH_NAD-bd.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   PROSITE; PS00065; D_2_HYDROXYACID_DH_1; FALSE_NEG.
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   Complete proteome; Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN         1    376       Formate dehydrogenase 1.
FT                                /FTId=PRO_0000223647.
FT   ACT_SITE    272    272       By similarity.
FT   ACT_SITE    325    325       Proton donor (By similarity).
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
//