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Reviewed, UniProtKB/Swiss-Prot Q06494 (PLR1_YEAST)

Last modified November 25, 2008. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Putative pyridoxal reductase
      Short name=PL reductase
      Short name=PL-red
    EC=1.1.1.65
Gene names
Ordered Locus Names: YPR127W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

Pathway

Cofactor degradation; B6 vitamer degradation; pyridoxal from pyridoxine (dehydrogenase route): step 1/1.

Subcellular location

Cytoplasm. Nucleus.

Miscellaneous

Present with 2190 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords

   Cellular componentCytoplasm
Nucleus
   LigandNADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm Ref.2

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus Ref.2

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpyridoxine 4-dehydrogenase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Putative pyridoxal reductase
PRO_0000257816

Sites

Active site601Proton donor By similarity

Amino acid modifications

Modified residue871Phosphoserine
Modified residue981Phosphothreonine

Sequences

Sequence LengthMass (Da)Tools
Q06494-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: C443ED79F25EA106

FASTA34538,601
        10         20         30         40         50         60 
MSVADLKNNI HKLDTGYGLM SLTWRAEPIP QSQAFEAMHR VVELSRERGH KAFFNVGEFY 

        70         80         90        100        110        120 
GPDFINLSYV HDFFAKYPDL RKDVVISCKG GADNATLTPR GSHDDVVQSV KNSVSAIGGY 

       130        140        150        160        170        180 
IDIFEVARID TSLCTKGEVY PYESFEALAE MISEGVIGGI SLSEVNEEQI RAIHKDWGKF 

       190        200        210        220        230        240 
LTCVEVELSL FSNDILHNGI AKTCAELGLS IICYSPLGRG LLTGQLKSNA DIPEGDFRKS 

       250        260        270        280        290        300 
LKRFSDESLK KNLTLVRFLQ EEIVDKRPQN NSITLAQLAL GWVKHWNKVP EYSGAKFIPI 

       310        320        330        340 
PSGSSISKVN ENFDEQKTKL TDQEFNAINK YLTTFHTVGD RYEMA 

« Hide

References

[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[2]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND THR-98, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

U40828 Genomic DNA. Translation: AAB68066.1.
PIRS69018.
RefSeqNP_015452.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ06494.

Proteomic databases

PeptideAtlasQ06494.

Genome annotation databases

EnsemblYPR127W. Saccharomyces cerevisiae. [Contig view]
GeneID856245.
GenomeReviewsGene locus YPR127W in contig U00094_GR.
KEGGsce:YPR127W.
NMPDRfig|4932.3.peg.6589.

Organism-specific databases

CYGDYPR127w.
SGDS000006331. YPR127W.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMQ06494.

Gene expression databases

GermOnlineYPR127W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
ProDomPD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00798. ALDOKETO_REDUCTASE_1. False negative.
PS00062. ALDOKETO_REDUCTASE_2. False negative.
PS00063. ALDOKETO_REDUCTASE_3. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubQ06494.
NextBio981513.

Entry information

Entry namePLR1_YEAST
AccessionPrimary (citable) accession number: Q06494
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: November 25, 2008
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents