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O94521 (PLR2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable pyridoxal reductase 2
Short name=PL reductase 2
Short name=PL-red 2
EC=1.1.1.65
Gene names
ORF Names:SPCC1281.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reduction of pyridoxal (PL) with NADPH and oxidation of pyridoxine (PN) with NADP+ By similarity.

Catalytic activity

Pyridoxine + NADP+ = pyridoxal + NADPH.

Subcellular location

Cytoplasm Ref.2.

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to stress

Inferred from expression pattern PubMed 12529438. Source: PomBase

pyridoxal biosynthetic process

Inferred from sequence or structural similarity. Source: PomBase

   Cellular_componentcytoplasm

Inferred from direct assay Ref.2. Source: PomBase

nucleus

Inferred from sequence orthology. Source: PomBase

   Molecular_functionpyridoxine:NADP 4-dehydrogenase activity

Inferred from sequence or structural similarity. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333Probable pyridoxal reductase 2
PRO_0000310315

Sites

Active site521Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
O94521 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: D69C0BEE8735E0F2

FASTA33336,844
        10         20         30         40         50         60 
MPIVNGFKVG PIGLGLMGLT WRPKQTPIKQ AFELMNYALS QGSNYWNAGE FYGINPPTAN 

        70         80         90        100        110        120 
LDLLADYFEK YPKNADKVFL SVKGGTDFKT LAPHGDPESV TKSVKNALTR LRGKKKLDLF 

       130        140        150        160        170        180 
QCARVDHKVP IETTMKALKA FVDSGEISCV GLSEASAESI KRALAIVPIA AVETEYSLFS 

       190        200        210        220        230        240 
RDIEKNGILD TCTQLSIPII AYAPFCHGLL TGRVKTAEDL KDFIKAFPFL RNMDKFNPKV 

       250        260        270        280        290        300 
FEKNIPFLKA VEQLAQKFGM SMPEFALNFI IANGKGMIIP IPGSTTVQRA ESNLSALKKS 

       310        320        330 
LSSEQLEEAK KVLDKHQIFG LRYNKQLEST LSI

« Hide

References

[1]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329672 Genomic DNA. Translation: CAA22825.1.
PIRT40923.
RefSeqNP_588168.1. NM_001023157.2.

3D structure databases

ProteinModelPortalO94521.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4684877.
STRING4896.SPCC1281.04-1.

Proteomic databases

PaxDbO94521.
PRIDEO94521.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1281.04.1; SPCC1281.04.1:pep; SPCC1281.04.
GeneID2539165.
KEGGspo:SPCC1281.04.

Organism-specific databases

PomBaseSPCC1281.04.

Phylogenomic databases

eggNOGCOG0667.
HOGENOMHOG000250284.
OMAANARSHR.
OrthoDBEOG4B8NP3.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. Aldo/ket_red.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERPTHR11732. PTHR11732. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
SUPFAMSSF51430. Aldo/ket_red. 1 hit.
PROSITEPS00798. ALDOKETO_REDUCTASE_1. False negative.
PS00062. ALDOKETO_REDUCTASE_2. False negative.
PS00063. ALDOKETO_REDUCTASE_3. False negative.
[Graphical view]
ProtoNetSearch...

Other

NextBio20800336.

Entry information

Entry namePLR2_SCHPO
AccessionPrimary (citable) accession number: O94521
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 1999
Last modified: May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

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