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P32263 (P5CR_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyrroline-5-carboxylate reductase

Short name=P5C reductase
Short name=P5CR
EC=1.5.1.2
Gene names
Name:PRO3
Synonyms:ORE2
Ordered Locus Names:YER023W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-proline + NAD(P)+ = 1-pyrroline-5-carboxylate + NAD(P)H.

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.

Subunit structure

Homotetramer.

Miscellaneous

Present with 43500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the pyrroline-5-carboxylate reductase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-13885,EBI-13885

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Pyrroline-5-carboxylate reductase
PRO_0000187328

Amino acid modifications

Modified residue2461Phosphothreonine Ref.7
Modified residue2791Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P32263 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: AEB71D93B46D08B3

FASTA28630,132
        10         20         30         40         50         60 
MTYTLAILGC GVMGQALLSA IYNAPKAADE TAAAFYPSKI ITCNHDEPSA QQVTDLVETF 

        70         80         90        100        110        120 
DESPNGIKVE STYGHNVSAV EEASVVLLGT KPFLAEEVLN GVKSVIGGKL LISLAAGWTI 

       130        140        150        160        170        180 
DQLSQYTSTV CRVMTNTPAK YGYGCAVVSY SADVSKEQKP LVNELISQVG KYVELPEKNM 

       190        200        210        220        230        240 
DAATALVGSG PAFVLLMLES LMESGLKLGI PLQESKECAM KVLEGTVKMV EKSGAHPSVL 

       250        260        270        280 
KHQVCTPGGT TIAGLCVMEE KGVKSGIING VEEAARVASQ LGQKKK 

« Hide

References

« Hide 'large scale' references
[1]"Proline biosynthesis in Saccharomyces cerevisiae: analysis of the PRO3 gene, which encodes delta 1-pyrroline-5-carboxylate reductase."
Brandriss M.C., Falvey D.A.
J. Bacteriol. 174:3782-3788(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Erratum
Brandriss M.C., Falvey D.A.
J. Bacteriol. 174:5176-5176(1992) [PubMed] [Europe PMC] [Abstract]
[3]"ore2, a mutation affecting proline biosynthesis in the yeast Saccharomyces cerevisiae, leads to a cdc phenotype."
Neuville P., Aigle M.
Mol. Gen. Genet. 234:193-200(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"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] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246 AND SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M57886 Genomic DNA. Translation: AAA34905.1.
X57338 Genomic DNA. Translation: CAA40614.1.
U18778 Genomic DNA. Translation: AAB64556.1.
BK006939 Genomic DNA. Translation: DAA07676.1.
PIRS25293.
RefSeqNP_010940.3. NM_001178914.3.

3D structure databases

ProteinModelPortalP32263.
SMRP32263. Positions 5-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36757. 32 interactions.
DIPDIP-1529N.
IntActP32263. 11 interactions.
MINTMINT-411759.
STRING4932.YER023W.

Proteomic databases

MaxQBP32263.
PaxDbP32263.
PeptideAtlasP32263.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER023W; YER023W; YER023W.
GeneID856744.
KEGGsce:YER023W.

Organism-specific databases

CYGDYER023w.
SGDS000000825. PRO3.

Phylogenomic databases

eggNOGCOG0345.
GeneTreeENSGT00390000007443.
HOGENOMHOG000230247.
KOK00286.
OMACCKPQQA.
OrthoDBEOG76DV3T.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-11544.
YEAST:YER023W-MONOMER.
UniPathwayUPA00098; UER00361.

Gene expression databases

GenevestigatorP32263.

Family and domain databases

Gene3D1.10.3730.10. 1 hit.
3.40.50.720. 1 hit.
InterProIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR029036. P5CR_dimer.
IPR028939. ProC_N.
IPR000304. Pyrroline-COOH_reductase.
[Graphical view]
PANTHERPTHR11645. PTHR11645. 1 hit.
PfamPF03807. F420_oxidored. 1 hit.
PF14748. P5CR_dimer. 1 hit.
[Graphical view]
PIRSFPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
SUPFAMSSF48179. SSF48179. 1 hit.
TIGRFAMsTIGR00112. proC. 1 hit.
PROSITEPS00521. P5CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio982882.
PROP32263.

Entry information

Entry nameP5CR_YEAST
AccessionPrimary (citable) accession number: P32263
Secondary accession number(s): D3DLS2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways