YGDH_SCHPO
ID YGDH_SCHPO Reviewed; 340 AA.
AC O94574; Q9HFE2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative 2-hydroxyacid dehydrogenase C1773.17c;
DE EC=1.-.-.-;
GN ORFNames=SPBC1773.17c, SPBP26C9.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21922.2; -; Genomic_DNA.
DR PIR; T39682; T39682.
DR RefSeq; NP_595132.2; NM_001021039.3.
DR AlphaFoldDB; O94574; -.
DR SMR; O94574; -.
DR BioGRID; 276695; 22.
DR STRING; 4896.SPBC1773.17c.1; -.
DR MaxQB; O94574; -.
DR PaxDb; O94574; -.
DR EnsemblFungi; SPBC1773.17c.1; SPBC1773.17c.1:pep; SPBC1773.17c.
DR GeneID; 2540160; -.
DR KEGG; spo:SPBC1773.17c; -.
DR PomBase; SPBC1773.17c; -.
DR VEuPathDB; FungiDB:SPBC1773.17c; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; O94574; -.
DR OMA; QMGDSMV; -.
DR PhylomeDB; O94574; -.
DR PRO; PR:O94574; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IBA:GO_Central.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; IC:PomBase.
DR GO; GO:0009436; P:glyoxylate catabolic process; ISO:PomBase.
DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR InterPro; IPR029753; D-isomer_DH_CS.
DR InterPro; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
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; PS00065; D_2_HYDROXYACID_DH_1; 1.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..340
FT /note="Putative 2-hydroxyacid dehydrogenase C1773.17c"
FT /id="PRO_0000076039"
FT ACT_SITE 251
FT /evidence="ECO:0000250"
FT ACT_SITE 280
FT /evidence="ECO:0000250"
FT ACT_SITE 298
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 169..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 249..251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 298..301
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 37658 MW; 44ED8DD371062043 CRC64;
MKQSRTKRVL AIGELKFATN TLKRLSEKYH FEFIVPDPHD RSKTIEKIHE AASKSTFDAC
FWLFRNAAIS PFTEEMLGPL LPTCKLFVTG AAGYNNVDVD WATRNGVYVA NTPNGPTEGT
ANMNLMLFMC TLRGAREAEQ SLRLGKWRQN LSLTDDPYGK RVGIIGMGAI GKSFAQKILP
LGCEIVYHNR NRLEAEEEKR LGASFVSFDE LLSSSDVISI NCPLTPATHD LISTKEFEKM
KDGVYIINTA RGAIINEDAF IKAIKSGKVA RAGLDVFLNE PTPNKFWLEC DKVTIQPHCG
VYTNFTVAKT EECVLASIET FLDTGIPTNP VNGPFGMNGC