Reviewed, UniProtKB/Swiss-Prot O14295 (PLR1_SCHPO)

Names and origin

Protein names

Recommended name:
    Pyridoxal reductase
      Short name=PL reductase
      Short name=PL-red
    EC=1.1.1.65

Gene names

Name:	plr1
Synonyms:	plr
ORF Names:	SPAC9E9.11

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	333 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP+.
Catalytic activity	Pyridoxine + NADP+ = pyridoxal + NADPH. Ref.3 Ref.4
Pathway	Cofactor degradation; B6 vitamer degradation; pyridoxal from pyridoxine (dehydrogenase route): step 1/1.
Subunit structure	Monomer. Ref.3 Ref.4
Subcellular location	Cytoplasm By similarity.
Post-translational modification	The N-terminus is blocked. Ref.3
Sequence similarities	Belongs to the aldo/keto reductase family.
Biophysicochemical properties	Kinetic parameters: KM=0.9 mM for pyridoxal Ref.3 Ref.4 pH dependence: Optimum pH is 6.5-7.5 for the reverse reaction. Ref.3 Ref.4

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cellular response to stress Inferred from expression pattern. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal biosynthetic process Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	pyridoxine 4-dehydrogenase activity Ref.3 Inferred from mutant phenotype. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 333	333	Pyridoxal reductase		PRO_0000124683
Sites
	Active site	52	1	Proton donor By similarity
Amino acid modifications
	Modified residue	292	1	Phosphoserine Ref.5
Experimental info
	Sequence conflict	92 – 102	11	VPDGNPDFVSK → FLVGNRTSFPR in BAA34350. Ref.1
	Sequence conflict	115	1	K → Q in BAA34350. Ref.1
	Sequence conflict	115	1	K → Q in BAA13866. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O14295-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: D4A3A2CE2046507D	FASTA	333	36,815
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of open reading frames in Schizosaccharomyces pombe cDNAs." Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H. DNA Res. 4:363-369(1997) [PubMed: 9501991] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: PR745.
[2]	"The genome sequence of Schizosaccharomyces pombe." 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. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Purification, molecular cloning, and catalytic activity of Schizosaccharomyces pombe pyridoxal reductase. A possible additional family in the aldo-keto reductase superfamily." Nakano M., Morita T., Yamamoto T., Sano H., Ashiuchi M., Masui R., Kuramitsu S., Yagi T. J. Biol. Chem. 274:23185-23190(1999) [PubMed: 10438489] [Abstract] Cited for: 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, SUBUNIT. Strain: IFO 0346.
[4]	"Purification and properties of pyridoxine oxidase from Aureobacterium luteolum and pyridoxal reductase from Schizosaccharomyces pombe." Yagi T., Ashiuchi M., Kaneda Y., Sano H. BioFactors 11:123-126(2000) [PubMed: 10705982] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22; 60-77; 104-136; 140-146; 222-225; 244-256; 272-280 AND 316-332, CATALYTIC ACTIVITY, SUBUNIT. Strain: IFO 0346.
[5]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB019429 mRNA. Translation: BAA34350.1. D89205 mRNA. Translation: BAA13866.1. CU329670 Genomic DNA. Translation: CAB16409.1.
PIR	T39218. T43436.
RefSeq	NP_594584.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O14295.
Genome annotation databases
GeneID	2542917.
GenomeReviews	Gene locus plr1 in contig CU329670_GR.
KEGG	spo:SPAC9E9.11.
NMPDR	fig|4896.1.peg.4554.
Organism-specific databases
GeneDB_Spombe	SPAC9E9.11.
Phylogenomic databases
OMA	CVEVELS.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002680-MON.
BRENDA	1.1.1.65. 653.
Gene expression databases
ArrayExpress	O14295.
Family and domain databases
InterPro	IPR001395. Aldo/ket_red. IPR018170. Aldo/ket_reductase_CS. [Graphical view]
Gene3D	G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHER	PTHR11732. Aldo/ket_red. 1 hit.
Pfam	PF00248. Aldo_ket_red. 1 hit. [Graphical view]
ProDom	PD000288. Aldo/ket_red. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00798. ALDOKETO_REDUCTASE_1. False negative. PS00062. ALDOKETO_REDUCTASE_2. False negative. PS00063. ALDOKETO_REDUCTASE_3. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLR1_SCHPO

Accession

Primary (citable) accession number: O14295
Secondary accession number(s): O94234, P78855

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)