FDH2_YEAST
ID FDH2_YEAST Reviewed; 236 AA.
AC P0CF35; Q08987; Q08988;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Truncated formate dehydrogenase 2 {ECO:0000305};
DE AltName: Full=NAD-dependent formate dehydrogenase 2 {ECO:0000303|PubMed:11921099};
GN Name=FDH2 {ECO:0000303|PubMed:11921099};
GN OrderedLocusNames=YPL275W {ECO:0000312|SGD:S000006196}; ORFNames=P0326;
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=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., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., 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., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64, AND CONFIRMATION OF STOP CODON.
RC STRAIN=ATCC 200060 / W303, and ATCC 201388 / BY4741;
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 -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. FDH subfamily. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene unlikely to encode a
CC functional protein. This is the C-terminal part of a second copy of
CC formate dehydrogenase in the yeast genome. Strains BY4741, S288c and
CC W303 have a stop codon in position 146, which disrupts the gene coding
CC for this protein and produces two ORFs YPL275W and YPL276W. Because of
CC that it is not part of the S.cerevisiae S288c complete/reference
CC proteome set. A contiguous sequence for formate dehydrogenase 2 can be
CC found in strain CEN.PK113-7D (AC P0CT22). {ECO:0000305|PubMed:11921099,
CC ECO:0000305|PubMed:24374639}.
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DR EMBL; Z73632; CAA98013.1; -; Genomic_DNA.
DR PIR; S65308; S65308.
DR AlphaFoldDB; P0CF35; -.
DR SMR; P0CF35; -.
DR DIP; DIP-3921N; -.
DR SGD; S000006196; FDH2.
DR VEuPathDB; FungiDB:YPL275W; -.
DR InParanoid; P0CF35; -.
DR GO; GO:0005829; C:cytosol; ISS:SGD.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IGI:SGD.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0042183; P:formate catabolic process; IGI:SGD.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
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 5: Uncertain;
KW NAD; Oxidoreductase.
FT CHAIN 1..236
FT /note="Truncated formate dehydrogenase 2"
FT /id="PRO_0000223648"
FT BINDING 36..37
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P33160"
FT BINDING 57
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P33160"
FT BINDING 104..108
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P33160"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P33160"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P33160"
FT BINDING 185..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P33160"
FT SITE 132
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P33160"
FT SITE 185
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P33160"
SQ SEQUENCE 236 AA; 26487 MW; 1C8E40684606D166 CRC64;
MVVINKQLMV SGILPAWLKN EYDLEDKIIS TVGAGRIGYR VLERLVAFNP KKLLYYDYQE
LPAEAINRLN EASKLFNGRG DIVQRVEKLE DMVAQSDVVT INCPLHKDSR GLFNKKLISH
MKDGAYLVNT ARGAICVAED VAEAVKSGKL AGYGGDVWDK QPAPKDHPWR TMDNKDHVGN
AMTVHISGTS LHAQKRYAQG VKNILNSYFS KKFDYRPQDI IVQNGSYATR AYGQKK
