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Database: UniProt
Entry: C8ZHD6
LinkDB: C8ZHD6
Original site: C8ZHD6 
ID   FDH1_YEAS8              Reviewed;         376 AA.
AC   C8ZHD6;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 46.
DE   RecName: Full=Formate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_03210};
DE            Short=FDH {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 {ECO:0000255|HAMAP-Rule:MF_03210};
GN   Name=FDH1; ORFNames=EC1118_1O4_6403g;
OS   Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse)
OS   (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=643680;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lalvin EC1118 / Prise de mousse;
RX   PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA   Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S.,
RA   Cambon B., Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT   "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT   sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(2009).
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. Has a
CC       role in the detoxification of exogenous formate in non-
CC       methylotrophic organisms. {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   -!- INDUCTION: Induced by formate.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. FDH subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03210}.
DR   EMBL; FN394216; CAY86665.1; -; Genomic_DNA.
DR   ProteinModelPortal; C8ZHD6; -.
DR   SMR; C8ZHD6; -.
DR   EnsemblFungi; CAY86665; CAY86665; EC1118_1O4_6403g.
DR   Proteomes; UP000000286; Chromosome XV, Scaffold EC1118_1O4.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Complete proteome; Cytoplasm; NAD; Oxidoreductase.
FT   CHAIN         1    376       Formate dehydrogenase 1.
FT                                /FTId=PRO_0000393442.
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}.
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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