ID   PLR1_SCHPO              Reviewed;         333 AA.
AC   O14295; O94234; P78855;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   16-JUN-2009, entry version 61.
DE   RecName: Full=Pyridoxal reductase;
DE            Short=PL reductase;
DE            Short=PL-red;
DE            EC=1.1.1.65;
GN   Name=plr1; Synonyms=plr; ORFNames=SPAC9E9.11;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=PR745;
RX   MEDLINE=98162722; 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=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-7; 9-22; 61-77; 104-114; 117-136; 140-146;
RP   222-225; 244-256; 271-280 AND 316-332, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
RC   STRAIN=IFO 0346;
RX   MEDLINE=99367443; PubMed=10438489; DOI=10.1074/jbc.274.33.23185;
RA   Nakano M., Morita T., Yamamoto T., Sano H., Ashiuchi M., Masui R.,
RA   Kuramitsu S., Yagi T.;
RT   "Purification, molecular cloning, and catalytic activity of
RT   Schizosaccharomyces pombe pyridoxal reductase. A possible additional
RT   family in the aldo-keto reductase superfamily.";
RL   J. Biol. Chem. 274:23185-23190(1999).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-22; 60-77; 104-136; 140-146; 222-225; 244-256;
RP   272-280 AND 316-332, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=IFO 0346;
RX   MEDLINE=20168499; PubMed=10705982;
RA   Yagi T., Ashiuchi M., Kaneda Y., Sano H.;
RT   "Purification and properties of pyridoxine oxidase from Aureobacterium
RT   luteolum and pyridoxal reductase from Schizosaccharomyces pombe.";
RL   BioFactors 11:123-126(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Catalyzes the reduction of pyridoxal (PL) with NADPH and
CC       oxidation of pyridoxine (PN) with NADP(+).
CC   -!- CATALYTIC ACTIVITY: Pyridoxine + NADP(+) = pyridoxal + NADPH.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.9 mM for pyridoxal;
CC       pH dependence:
CC         Optimum pH is 6.5-7.5 for the reverse reaction;
CC   -!- PATHWAY: Cofactor degradation; B6 vitamer degradation; pyridoxal
CC       from pyridoxine (dehydrogenase route): step 1/1.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family.
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DR   EMBL; AB019429; BAA34350.1; -; mRNA.
DR   EMBL; D89205; BAA13866.1; -; mRNA.
DR   EMBL; CU329670; CAB16409.1; -; Genomic_DNA.
DR   PIR; T39218; T39218.
DR   PIR; T43436; T43436.
DR   RefSeq; NP_594584.1; -.
DR   GeneID; 2542917; -.
DR   KEGG; spo:SPAC9E9.11; -.
DR   NMPDR; fig|4896.1.peg.4554; -.
DR   GeneDB_Spombe; SPAC9E9.11; -.
DR   OMA; O14295; CVEVELS.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002680-MON; -.
DR   BRENDA; 1.1.1.65; 653.
DR   ArrayExpress; O14295; -.
DR   GO; GO:0005829; C:cytosol; IDA:GeneDB_SPombe.
DR   GO; GO:0005634; C:nucleus; IDA:GeneDB_SPombe.
DR   GO; GO:0050236; F:pyridoxine 4-dehydrogenase activity; IMP:GeneDB_SPombe.
DR   GO; GO:0033554; P:cellular response to stress; IEP:GeneDB_SPombe.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0042821; P:pyridoxal biosynthetic process; IMP:GeneDB_SPombe.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   InterPro; IPR018170; Aldo/ket_reductase_CS.
DR   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   ProDom; PD000288; Aldo/ket_red; 1.
DR   PROSITE; PS00798; ALDOKETO_REDUCTASE_1; FALSE_NEG.
DR   PROSITE; PS00062; ALDOKETO_REDUCTASE_2; FALSE_NEG.
DR   PROSITE; PS00063; ALDOKETO_REDUCTASE_3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Direct protein sequencing; NADP;
KW   Oxidoreductase; Phosphoprotein.
FT   CHAIN         1    333       Pyridoxal reductase.
FT                                /FTId=PRO_0000124683.
FT   ACT_SITE     52     52       Proton donor (By similarity).
FT   MOD_RES     292    292       Phosphoserine.
FT   CONFLICT     92    102       VPDGNPDFVSK -> FLVGNRTSFPR (in Ref. 1;
FT                                BAA34350).
FT   CONFLICT    115    115       K -> Q (in Ref. 1; BAA34350/BAA13866).
SQ   SEQUENCE   333 AA;  36815 MW;  D4A3A2CE2046507D CRC64;
     MPIVSGFKVG PIGFGLMGLT WKPKQTPDEE AFEVMNYALS QGSNYWDAGE FYGVDPPTSN
     LDLLARYFEK YPENANKVFL SVKGGLDFKT LVPDGNPDFV SKSVENVIAH LRGTKKLDLF
     QCARVDPNVP IETTMKTLKG FVDSGKISCV GLSEVSAETI KRAHAVVPIA AVEVEYSLFS
     RDIETNGIMD ICRKLSIPII AYSPFCRGLL TGRIKTVEDL KEFAKSFPFL EYLDRFSPDV
     FAKNLPFLQA VEQLAKKFGM TMPEFSLLFI MASGNGLVIP IPGSTSVSRT KSNLNALNKS
     LSPEQFKEAK EVLSKYPIYG LRYNEQLAGT LSV
//