ID   P5CR_YEAST              Reviewed;         286 AA.
AC   P32263;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   04-NOV-2008, entry version 69.
DE   RecName: Full=Pyrroline-5-carboxylate reductase;
DE            Short=P5C reductase;
DE            Short=P5CR;
DE            EC=1.5.1.2;
GN   Name=PRO3; Synonyms=ORE2; OrderedLocusNames=YER023W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92276362; PubMed=1592829;
RA   Brandriss M.C., Falvey D.A.;
RT   "Proline biosynthesis in Saccharomyces cerevisiae: analysis of the
RT   PRO3 gene, which encodes delta 1-pyrroline-5-carboxylate reductase.";
RL   J. Bacteriol. 174:3782-3788(1992).
RN   [2]
RP   ERRATUM.
RX   MEDLINE=92332464; PubMed=1352771;
RA   Brandriss M.C., Falvey D.A.;
RL   J. Bacteriol. 174:5176-5176(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92374987; PubMed=1508147; DOI=10.1007/BF00283839;
RA   Neuville P., Aigle M.;
RT   "ore2, a mutation affecting proline biosynthesis in the yeast
RT   Saccharomyces cerevisiae, leads to a cdc phenotype.";
RL   Mol. Gen. Genet. 234:193-200(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   MEDLINE=97313264; PubMed=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G.,
RA   Hunicke-Smith S., Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H.,
RA   Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P.,
RA   Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T.,
RA   Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246 AND SER-279, AND
RP   MASS SPECTROMETRY.
RX   PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
CC   -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5-
CC       carboxylate + NAD(P)H.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       proline from L-glutamate 5-semialdehyde: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-13885, EBI-13885;
CC       Q99257:MEX67; NbExp=1; IntAct=EBI-13885, EBI-11642;
CC   -!- MISCELLANEOUS: Present with 43500 molecules/cell in log phase SD
CC       medium.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M57886; AAA34905.1; -; Genomic_DNA.
DR   EMBL; X57338; CAA40614.1; -; Genomic_DNA.
DR   EMBL; U18778; AAB64556.1; -; Genomic_DNA.
DR   PIR; S25293; S25293.
DR   RefSeq; NP_010940.1; -.
DR   DIP; DIP:1529N; -.
DR   IntAct; P32263; -.
DR   PeptideAtlas; P32263; -.
DR   Ensembl; YER023W; Saccharomyces cerevisiae.
DR   GeneID; 856744; -.
DR   GenomeReviews; U00092_GR; YER023W.
DR   KEGG; sce:YER023W; -.
DR   NMPDR; fig|4932.3.peg.2000; -.
DR   CYGD; YER023w; -.
DR   SGD; S000000825; PRO3.
DR   HOGENOM; P32263; -.
DR   BioCyc; MetaCyc:MON-11544; -.
DR   LinkHub; P32263; -.
DR   NextBio; 982882; -.
DR   GermOnline; YER023W; Saccharomyces cerevisiae.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IGI:SGD.
DR   GO; GO:0006561; P:proline biosynthetic process; IMP:SGD.
DR   InterPro; IPR004455; NADP_OxRdtase_F420.
DR   InterPro; IPR000304; P5CR.
DR   PANTHER; PTHR11645; P5CR; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   TIGRFAMs; TIGR00112; proC; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Complete proteome; NADP; Oxidoreductase;
KW   Phosphoprotein; Proline biosynthesis.
FT   CHAIN         1    286       Pyrroline-5-carboxylate reductase.
FT                                /FTId=PRO_0000187328.
FT   MOD_RES     246    246       Phosphothreonine.
FT   MOD_RES     279    279       Phosphoserine.
SQ   SEQUENCE   286 AA;  30132 MW;  AEB71D93B46D08B3 CRC64;
     MTYTLAILGC GVMGQALLSA IYNAPKAADE TAAAFYPSKI ITCNHDEPSA QQVTDLVETF
     DESPNGIKVE STYGHNVSAV EEASVVLLGT KPFLAEEVLN GVKSVIGGKL LISLAAGWTI
     DQLSQYTSTV CRVMTNTPAK YGYGCAVVSY SADVSKEQKP LVNELISQVG KYVELPEKNM
     DAATALVGSG PAFVLLMLES LMESGLKLGI PLQESKECAM KVLEGTVKMV EKSGAHPSVL
     KHQVCTPGGT TIAGLCVMEE KGVKSGIING VEEAARVASQ LGQKKK
//