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UniProtKB/Swiss-Prot entry O14295


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PLR1_SCHPO
Primary accession number O14295
Secondary accession numbers O94234 P78855
Integrated into Swiss-Prot on November 1, 2002
Sequence was last modified on January 1, 1998 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 55)
Name and origin of the protein
Protein name Pyridoxal reductase
Synonyms PL reductase
PL-red
EC 1.1.1.65
Gene name
Name: plr1
Synonyms: plr
ORFNames: SPAC9E9.11
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=PR745;
DOI=10.1093/dnares/4.6.363; PubMed=9501991 [NCBI, ExPASy, EBI, Israel, Japan]
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
"Identification of open reading frames in Schizosaccharomyces pombe cDNAs.";
DNA Res. 4:363-369(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
PROTEIN SEQUENCE OF 2-7; 9-22; 61-77; 104-114; 117-136; 140-146; 222-225; 244-256; 271-280 AND 316-332, CATALYTIC ACTIVITY, AND SUBUNIT.
STRAIN=IFO 0346;
DOI=10.1074/jbc.274.33.23185; PubMed=10438489 [NCBI, ExPASy, EBI, Israel, Japan]
Nakano M., Morita T., Yamamoto T., Sano H., Ashiuchi M., Masui R., Kuramitsu S., Yagi T.;
"Purification, molecular cloning, and catalytic activity of Schizosaccharomyces pombe pyridoxal reductase. A possible additional family in the aldo-keto reductase superfamily.";
J. Biol. Chem. 274:23185-23190(1999).
[4]
PROTEIN SEQUENCE OF 2-22; 60-77; 104-136; 140-146; 222-225; 244-256; 272-280 AND 316-332, CATALYTIC ACTIVITY, AND SUBUNIT.
STRAIN=IFO 0346;
PubMed=10705982 [NCBI, ExPASy, EBI, Israel, Japan]
Yagi T., Ashiuchi M., Kaneda Y., Sano H.;
"Purification and properties of pyridoxine oxidase from Aureobacterium luteolum and pyridoxal reductase from Schizosaccharomyces pombe.";
BioFactors 11:123-126(2000).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND MASS SPECTROMETRY.
DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan]
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB019429; BAA34350.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D89205; BAA13866.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAB16409.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39218; T39218.
T43436; T43436.
RefSeq NP_594584.1; -.
3D structure databases
ModBase O14295.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-002680-MON; -.
Organism-specific databases
GeneDB_Spombe SPAC9E9.11; -.
Gene expression databases
ArrayExpress O14295; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0016020; Cellular component: membrane (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from direct assay from GeneDB_SPombe).
GO:0050236; Molecular function: pyridoxine 4-dehydrogenase activity (inferred from mutant phenotype from GeneDB_SPombe).
GO:0042821; Biological process: pyridoxal biosynthetic process (inferred from mutant phenotype from GeneDB_SPombe).
QuickGo view.
Family and domain databases
InterPro IPR001395; Aldo/ket_red.
Graphical view of domain structure.
Gene3D G3DSA:3.20.20.100; Aldo/ket_red; 1.
PANTHER PTHR11732; Aldo/ket_red; 1.
Pfam PF00248; Aldo_ket_red; 1.
Pfam graphical view of domain structure.
ProDom PD000288; Aldo/ket_red; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00798; ALDOKETO_REDUCTASE_1; FALSE_NEG.
PS00062; ALDOKETO_REDUCTASE_2; FALSE_NEG.
PS00063; ALDOKETO_REDUCTASE_3; FALSE_NEG.
BLOCKS O14295.
Genome annotation databases
GeneID 2542917; -.
KEGG spo:SPAC9E9.11; -.
NMPDR fig|4896.1.peg.4554; -.
Other
ProtoNet O14295.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Direct protein sequencing; NADP; Oxidoreductase; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   333  333     Pyridoxal reductase. PRO_0000124683
ACT_SITE   52    52        Proton donor (By similarity). 
MOD_RES   292   292        Phosphoserine. 
CONFLICT   92   102        VPDGNPDFVSK -> FLVGNRTSFPR (in Ref. 1; BAA34350). 
CONFLICT   115   115        K -> Q (in Ref. 1; BAA34350/BAA13866). 
Sequence information
Length: 333 AA [This is the length of the unprocessed precursor] Molecular weight: 36815 Da [This is the MW of the unprocessed precursor] CRC64: D4A3A2CE2046507D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPIVSGFKVG PIGFGLMGLT WKPKQTPDEE AFEVMNYALS QGSNYWDAGE FYGVDPPTSN 

        70         80         90        100        110        120 
LDLLARYFEK YPENANKVFL SVKGGLDFKT LVPDGNPDFV SKSVENVIAH LRGTKKLDLF 

       130        140        150        160        170        180 
QCARVDPNVP IETTMKTLKG FVDSGKISCV GLSEVSAETI KRAHAVVPIA AVEVEYSLFS 

       190        200        210        220        230        240 
RDIETNGIMD ICRKLSIPII AYSPFCRGLL TGRIKTVEDL KEFAKSFPFL EYLDRFSPDV 

       250        260        270        280        290        300 
FAKNLPFLQA VEQLAKKFGM TMPEFSLLFI MASGNGLVIP IPGSTSVSRT KSNLNALNKS 

       310        320        330 
LSPEQFKEAK EVLSKYPIYG LRYNEQLAGT LSV 

O14295 in FASTA format

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