PLR1_SCHPO
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 03-AUG-2022, entry version 142.
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 (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).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-7; 9-22; 61-77; 104-114; 117-136; 140-146; 222-225;
RP 244-256; 271-280 AND 316-332, CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=IFO 0346;
RX 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 family
RT in the aldo-keto reductase superfamily.";
RL J. Biol. Chem. 274:23185-23190(1999).
RN [4] {ECO:0000305}
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 PubMed=10705982; DOI=10.1002/biof.5520110137;
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 IDENTIFICATION BY
RP MASS 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:
CC Reaction=NADP(+) + pyridoxine = H(+) + NADPH + pyridoxal;
CC Xref=Rhea:RHEA:16129, ChEBI:CHEBI:15378, ChEBI:CHEBI:16709,
CC ChEBI:CHEBI:17310, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.65;
CC Evidence={ECO:0000269|PubMed:10438489, ECO:0000269|PubMed:10705982};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.9 mM for pyridoxal {ECO:0000269|PubMed:10438489,
CC ECO:0000269|PubMed:10705982};
CC pH dependence:
CC Optimum pH is 6.5-7.5 for the reverse reaction.
CC {ECO:0000269|PubMed:10438489, ECO:0000269|PubMed:10705982};
CC -!- PATHWAY: Cofactor degradation; B6 vitamer degradation; pyridoxal from
CC pyridoxine (dehydrogenase route): step 1/1.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10438489,
CC ECO:0000269|PubMed:10705982}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10438489}.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. {ECO:0000305}.
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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; NM_001020013.2.
DR AlphaFoldDB; O14295; -.
DR SMR; O14295; -.
DR BioGRID; 279358; 11.
DR STRING; 4896.SPAC9E9.11.1; -.
DR iPTMnet; O14295; -.
DR MaxQB; O14295; -.
DR PaxDb; O14295; -.
DR PRIDE; O14295; -.
DR EnsemblFungi; SPAC9E9.11.1; SPAC9E9.11.1:pep; SPAC9E9.11.
DR GeneID; 2542917; -.
DR KEGG; spo:SPAC9E9.11; -.
DR PomBase; SPAC9E9.11; plr1.
DR VEuPathDB; FungiDB:SPAC9E9.11; -.
DR eggNOG; KOG1575; Eukaryota.
DR HOGENOM; CLU_023205_2_1_1; -.
DR InParanoid; O14295; -.
DR OMA; MTMAYGA; -.
DR PhylomeDB; O14295; -.
DR BRENDA; 1.1.1.65; 5613.
DR SABIO-RK; O14295; -.
DR UniPathway; UPA00192; UER00307.
DR PRO; PR:O14295; -.
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; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
DR GO; GO:0050236; F:pyridoxine:NADP 4-dehydrogenase activity; IMP:PomBase.
DR GO; GO:0042821; P:pyridoxal biosynthetic process; IMP:PomBase.
DR GO; GO:0042820; P:vitamin B6 catabolic process; IEA:UniProtKB-UniPathway.
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 Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..333
FT /note="Pyridoxal reductase"
FT /id="PRO_0000124683"
FT ACT_SITE 52
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 92..102
FT /note="VPDGNPDFVSK -> FLVGNRTSFPR (in Ref. 1; BAA34350)"
FT /evidence="ECO:0000305"
FT CONFLICT 115
FT /note="K -> Q (in Ref. 1; BAA34350/BAA13866)"
FT /evidence="ECO:0000305"
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
