ID   FDH2_YEAST              Reviewed;         376 AA.
AC   Q08987; Q08988;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Formate dehydrogenase 2;
DE            EC=1.2.1.2;
DE   AltName: Full=NAD-dependent formate dehydrogenase 2;
GN   Name=FDH2; OrderedLocusNames=YPL275W/YPL276W; ORFNames=P0323/P0326;
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 204511 / S288c / AB972;
RX   MEDLINE=97313271; PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
RA   Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
RA   Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
RA   Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
RA   Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
RA   Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
RA   Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
RA   Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
RA   Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
RA   Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
RA   Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
RA   Zollner A., Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-145.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-204, FUNCTION, SUBCELLULAR
RP   LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 200060 / W303, ATCC 201388 / BY4741, and CEN.PK 113-7D;
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   -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: Induced by formate.
CC   -!- MISCELLANEOUS: Strains BY4741, S288c and W303 have a stop codon in
CC       position 146, which disrupts the gene coding for this protein and
CC       produces two ORFs.
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DR   EMBL; Z73632; CAA98012.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; Z73632; CAA98013.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY558055; AAS56381.1; ALT_SEQ; Genomic_DNA.
DR   PIR; S65308; S65308.
DR   PIR; S65309; S65309.
DR   HSSP; P33160; 2NAD.
DR   DIP; DIP:3921N; -.
DR   IntAct; Q08987; 2.
DR   Ensembl; YOR388C; Saccharomyces cerevisiae.
DR   CYGD; YPL275w; -.
DR   CYGD; YPL276w; -.
DR   SGD; S000006196; FDH2.
DR   SGD; S000006197; YPL276W.
DR   BRENDA; 1.2.1.2; 250.
DR   GermOnline; YOR388C; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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 2.
FT                                /FTId=PRO_0000223648.
FT   ACT_SITE    272    272       By similarity.
FT   ACT_SITE    325    325       Proton donor (By similarity).
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
//