ID   DDH1_SCHPO              Reviewed;         332 AA.
AC   Q9P7P8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=2-hydroxyacid dehydrogenase homolog 1;
DE            EC=1.1.1.-;
GN   ORFNames=SPAC186.07c;
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   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. {ECO:0000305}.
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DR   EMBL; CU329670; CAB75871.1; -; Genomic_DNA.
DR   PIR; T50134; T50134.
DR   RefSeq; NP_595025.1; NM_001020455.1.
DR   AlphaFoldDB; Q9P7P8; -.
DR   SMR; Q9P7P8; -.
DR   STRING; 4896.SPAC186.07c.1; -.
DR   PaxDb; Q9P7P8; -.
DR   EnsemblFungi; SPAC186.07c.1; SPAC186.07c.1:pep; SPAC186.07c.
DR   GeneID; 2542600; -.
DR   KEGG; spo:SPAC186.07c; -.
DR   PomBase; SPAC186.07c; -.
DR   VEuPathDB; FungiDB:SPAC186.07c; -.
DR   eggNOG; KOG0068; Eukaryota.
DR   HOGENOM; CLU_019796_1_1_1; -.
DR   InParanoid; Q9P7P8; -.
DR   OMA; TAYYTDH; -.
DR   PhylomeDB; Q9P7P8; -.
DR   PRO; PR:Q9P7P8; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
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; IEA:InterPro.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NAD; Nucleus; Oxidoreductase; Reference proteome.
FT   CHAIN           1..332
FT                   /note="2-hydroxyacid dehydrogenase homolog 1"
FT                   /id="PRO_0000316030"
FT   ACT_SITE        235
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        264
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        296
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         154..155
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         233..235
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         259
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         296..299
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   332 AA;  36589 MW;  55D0127B63DDC00C CRC64;
     MRIAFFSAQP YEKEPFEKVN ENYKHEIDYH ESILNKKTAV LAEKAPVVCV FVNDKVDADT
     LKVLAKNGTK LIALRCAGFN NVDLKAAADN GITVVRVPAY SPYAVAEYTI GLLLSLNRKI
     HRAYVRVRED DFNLNGLLGH DLHGKTIGLL GTGRIGGLVA KCLKLGFGCE VLAHDIKPNK
     ELEKFGIQFV EQQEVLAKAD FLCLHCPLTP DTEHLVDEKL LASMKKGVKI INTSRGGLVD
     TKALVKAIES GQVGGCAMDV YEGERRLFYR DLSNEVIKDT TFQQLANFPN VLVTSHQAFF
     TAEALSAIAH TTLKNVSDFA SQNNDPSVIV KN