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Database: UniProt
Entry: O14075
LinkDB: O14075
Original site: O14075 
ID   YEAA_SCHPO              Reviewed;         334 AA.
AC   O14075; P78836;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JAN-2019, entry version 129.
DE   RecName: Full=Putative 2-hydroxyacid dehydrogenase UNK4.10;
DE            EC=1.-.-.-;
GN   ORFNames=SPAC2E11.10, SPACUNK4.10;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=PR745;
RX   PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA   Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT   "Identification of open reading frames in Schizosaccharomyces pombe
RT   cDNAs.";
RL   DNA Res. 4:363-369(1997).
RN   [2]
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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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}.
DR   EMBL; D89185; BAA13847.1; -; mRNA.
DR   EMBL; CU329670; CAA20140.1; -; Genomic_DNA.
DR   PIR; T41705; T41705.
DR   PIR; T42743; T42743.
DR   RefSeq; NP_593968.1; NM_001019395.2.
DR   ProteinModelPortal; O14075; -.
DR   SMR; O14075; -.
DR   BioGrid; 279048; 10.
DR   STRING; 4896.SPACUNK4.10.1; -.
DR   iPTMnet; O14075; -.
DR   MaxQB; O14075; -.
DR   PaxDb; O14075; -.
DR   PRIDE; O14075; -.
DR   EnsemblFungi; SPACUNK4.10.1; SPACUNK4.10.1:pep; SPACUNK4.10.
DR   GeneID; 2542594; -.
DR   KEGG; spo:SPACUNK4.10; -.
DR   EuPathDB; FungiDB:SPACUNK4.10; -.
DR   PomBase; SPACUNK4.10; -.
DR   HOGENOM; HOG000136700; -.
DR   InParanoid; O14075; -.
DR   KO; K00015; -.
DR   OMA; PHIAWAY; -.
DR   PhylomeDB; O14075; -.
DR   Reactome; R-SPO-389661; Glyoxylate metabolism and glycine degradation.
DR   PRO; PR:O14075; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0047964; F:glyoxylate reductase activity; ISO:PomBase.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome.
FT   CHAIN         1    334       Putative 2-hydroxyacid dehydrogenase
FT                                UNK4.10.
FT                                /FTId=PRO_0000076038.
FT   NP_BIND     166    167       NAD. {ECO:0000250}.
FT   NP_BIND     244    246       NAD. {ECO:0000250}.
FT   NP_BIND     293    296       NAD. {ECO:0000250}.
FT   ACT_SITE    246    246       {ECO:0000250}.
FT   ACT_SITE    275    275       {ECO:0000250}.
FT   ACT_SITE    293    293       Proton donor. {ECO:0000250}.
FT   BINDING     270    270       NAD. {ECO:0000250}.
FT   CONFLICT     69     69       F -> W (in Ref. 1; BAA13847).
FT                                {ECO:0000305}.
SQ   SEQUENCE   334 AA;  36701 MW;  493BB4A28DDB4BFF CRC64;
     MTLSGKPAAL LVGTLKHAHK EWEALGKYAE LKTYSDGTRE DFLAKCKTEF QNVKAICRTY
     NSKFYMGIFD KEIIDNLPPS VKFICHLGAG YETVDVAACT ARGIQVSHVP KAVDDATADV
     GIFLMLGALR GFNQGIFELH KNNWNANCKP SHDPEGKTLG ILGLGGIGKT MAKRARAFDM
     KIVYHNRTPL PEEEAEGAEF VSFDDLLAKS DVLSLNLPLN AHTRHIIGKP EFQKMKRGIV
     IVNTARGAVM DEAALVEALD EGIVYSAGLD VFEEEPKIHP GLLENEKVIL LPHLGTNSLE
     TQYKMECAVL MNVKNGIVND SLPNLVPEQR GDIE
//
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