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   28-JUN-2023, entry version 62.
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};
GN   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   AGR; SGD:S000006196; -.
DR   SGD; S000006196; FDH2.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42938; FORMATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR42938:SF9; FORMATE DEHYDROGENASE 1; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 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
//