[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=1592829 [NCBI, ExPASy, EBI, Israel, Japan] Brandriss M.C., Falvey D.A.; "Proline biosynthesis in Saccharomyces cerevisiae: analysis of the PRO3 gene, which encodes delta 1-pyrroline-5-carboxylate reductase."; J. Bacteriol. 174:3782-3788(1992).
[2]	ERRATUM. PubMed=1352771 [NCBI, ExPASy, EBI, Israel, Japan] Brandriss M.C., Falvey D.A.; J. Bacteriol. 174:5176-5176(1992).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1007/BF00283839; PubMed=1508147 [NCBI, ExPASy, EBI, Israel, Japan] Neuville P., Aigle M.; "ore2, a mutation affecting proline biosynthesis in the yeast Saccharomyces cerevisiae, leads to a cdc phenotype."; Mol. Gen. Genet. 234:193-200(1992).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169868 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome V."; Nature 387:78-81(1997).
[5]	LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan] Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.; "Global analysis of protein expression in yeast."; Nature 425:737-741(2003).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246 AND SER-279, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 0:0-0(2008).

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: Homotetramer.
INTERACTION:
Self; NbExp=1; IntAct=EBI-13885, EBI-13885;
Q99257:MEX67; NbExp=1; IntAct=EBI-13885, EBI-11642;
MISCELLANEOUS: Present with 43500 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.

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

M57886; AAA34905.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57338; CAA40614.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U18778; AAB64556.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S25293; S25293.

RefSeq

NP_010940.1; -.

3D structure databases

ModBase

P32263.

Protein-protein interaction databases

DIP

DIP:1529N; -.

IntAct

P32263; -.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-11544; -.

Organism-specific databases

YER023w; -.

S000000825; PRO3.

Gene expression databases

GermOnline

YER023W; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004735;	Molecular function: pyrroline-5-carboxylate reductase activity (inferred from genetic interaction from SGD).
GO:0006561;	Biological process: proline biosynthetic process (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR004455; NADP_OxRdtase_F420.
IPR000304; P5CR.
Graphical view of domain structure.

PANTHER

PTHR11645; P5CR; 1.

Pfam

PF03807; F420_oxidored; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000193; Pyrrol-5-carb_rd; 1.

TIGR00112; proC; 1.

PS00521; P5CR; 1.

Proteomic databases

P32263; -.

Genome annotation databases

Ensembl

YER023W; Saccharomyces cerevisiae. [Contig view]

856744; -.

U00092_GR; YER023W.

sce:YER023W; -.

fig|4932.3.peg.2000; -.

Phylogenomic databases

HOGENOM

P32263; -.

Other

P32263; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Complete proteome; NADP; Oxidoreductase; Phosphoprotein; Proline biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 286`	`286`	`Pyrroline-5-carboxylate reductase.`	`PRO_0000187328`
`MOD_RES`	`246 246`		`Phosphothreonine.`
`MOD_RES`	`279 279`		`Phosphoserine.`

Sequence information

Length: 286 AA [This is the length of the unprocessed precursor]

Molecular weight: 30132 Da [This is the MW of the unprocessed precursor]

CRC64: AEB71D93B46D08B3 [This is a checksum on the sequence]

        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

P32263 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools