YEAA_SCHPO
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 03-AUG-2022, entry version 144.
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; Schizosaccharomycetaceae;
OC 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., 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; 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 AlphaFoldDB; O14075; -.
DR SMR; O14075; -.
DR BioGRID; 279048; 11.
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 PomBase; SPACUNK4.10; -.
DR VEuPathDB; FungiDB:SPACUNK4.10; -.
DR eggNOG; KOG0069; Eukaryota.
DR HOGENOM; CLU_019796_1_2_1; -.
DR InParanoid; O14075; -.
DR OMA; VHHQTLG; -.
DR PhylomeDB; O14075; -.
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: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 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..334
FT /note="Putative 2-hydroxyacid dehydrogenase UNK4.10"
FT /id="PRO_0000076038"
FT ACT_SITE 246
FT /evidence="ECO:0000250"
FT ACT_SITE 275
FT /evidence="ECO:0000250"
FT ACT_SITE 293
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 166..167
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 244..246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 293..296
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT CONFLICT 69
FT /note="F -> W (in Ref. 1; BAA13847)"
FT /evidence="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
