ID   YAKC_SCHPO              Reviewed;         340 AA.
AC   Q09923;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Aldo-keto reductase yakc [NADP(+)];
DE            EC=1.1.1.-;
GN   Name=yakc; ORFNames=SPAC1F7.12, SPAC21E11.01;
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 [GENOMIC DNA], PROTEIN SEQUENCE OF 34-56; 78-87;
RP   89-113; 147-157; 179-187; 191-224; 228-247; 289-311 AND 318-340, HYDROGEN
RP   DONOR, AND SUBUNIT.
RX   PubMed=12359080; DOI=10.1093/oxfordjournals.jbchem.a003267;
RA   Morita T., Huruta T., Ashiuchi M., Yagi T.;
RT   "Characterization of recombinant YakC of Schizosaccharomyces pombe showing
RT   YakC defines a new family of aldo-keto reductases.";
RL   J. Biochem. 132:635-641(2002).
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   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12359080}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. Aldo/keto
CC       reductase 2 subfamily. {ECO:0000305}.
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DR   EMBL; CU329670; CAA91959.1; -; Genomic_DNA.
DR   PIR; S62584; S62584.
DR   RefSeq; NP_594498.1; NM_001019927.2.
DR   AlphaFoldDB; Q09923; -.
DR   SMR; Q09923; -.
DR   STRING; 4896.SPAC1F7.12.1; -.
DR   MaxQB; Q09923; -.
DR   PaxDb; Q09923; -.
DR   EnsemblFungi; SPAC1F7.12.1; SPAC1F7.12.1:pep; SPAC1F7.12.
DR   GeneID; 2541648; -.
DR   KEGG; spo:SPAC1F7.12; -.
DR   PomBase; SPAC1F7.12; -.
DR   VEuPathDB; FungiDB:SPAC1F7.12; -.
DR   eggNOG; KOG1575; Eukaryota.
DR   HOGENOM; CLU_023205_2_1_1; -.
DR   InParanoid; Q09923; -.
DR   OMA; MHRRDPA; -.
DR   PhylomeDB; Q09923; -.
DR   PRO; PR:Q09923; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IDA:PomBase.
DR   Gene3D; 3.20.20.100; -; 1.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   SUPFAM; SSF51430; SSF51430; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..340
FT                   /note="Aldo-keto reductase yakc [NADP(+)]"
FT                   /id="PRO_0000070398"
FT   ACT_SITE        56
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         208..218
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            83
FT                   /note="Lowers pKa of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   340 AA;  37710 MW;  A4A9686A70968F06 CRC64;
     MSIPTRKIGN DTVPAIGFGC MGLHAMYGPS SEEANQAVLT HAADLGCTFW DSSDMYGFGA
     NEECIGRWFK QTGRRKEIFL ATKFGYEKNP ETGELSLNNE PDYIEKALDL SLKRLGIDCI
     DLYYVHRFSG ETPIEKIMGA LKKCVEAGKI RYIGLSECSA NTIRRAAAVY PVSAVQVEYS
     PFSLEIERPE IGVMKACREN NITIVCYAPL GRGFLTGAYK SPDDFPEGDF RRKAPRYQKE
     NFYKNLELVT KIEKIATANN ITPGQLSLAW LLAQGDDILP IPGTKRVKYL EENFGALKVK
     LSDATVKEIR EACDNAEVIG ARYPPGAGSK IFMDTPPMPK