P5CR_YEAST
ID P5CR_YEAST Reviewed; 286 AA.
AC P32263; D3DLS2;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Pyrroline-5-carboxylate reductase;
DE Short=P5C reductase;
DE Short=P5CR;
DE EC=1.5.1.2 {ECO:0000269|PubMed:1592829};
GN Name=PRO3 {ECO:0000303|PubMed:1592829};
GN Synonyms=ORE2 {ECO:0000303|PubMed:1508147}; OrderedLocusNames=YER023W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1592829; DOI=10.1128/jb.174.11.3782-3788.1992;
RA Brandriss M.C., Falvey D.A.;
RT "Proline biosynthesis in Saccharomyces cerevisiae: analysis of the PRO3
RT gene, which encodes delta 1-pyrroline-5-carboxylate reductase.";
RL J. Bacteriol. 174:3782-3788(1992).
RN [2]
RP ERRATUM OF PUBMED:1592829.
RX PubMed=1352771; DOI=10.1128/jb.174.15.5176b.1992;
RA Brandriss M.C., Falvey D.A.;
RL J. Bacteriol. 174:5176-5176(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1508147; DOI=10.1007/bf00283839;
RA Neuville P., Aigle M.;
RT "ore2, a mutation affecting proline biosynthesis in the yeast Saccharomyces
RT 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 204508 / S288c;
RX 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., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246 AND SER-279, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-171, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline, the final step in proline biosynthesis.
CC {ECO:0000305|PubMed:1592829}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000305|PubMed:1592829};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14111;
CC Evidence={ECO:0000305|PubMed:1592829};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000269|PubMed:1592829};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:14107;
CC Evidence={ECO:0000269|PubMed:1592829};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {ECO:0000305|PubMed:1508147}.
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P32263; P32263: PRO3; NbExp=3; IntAct=EBI-13885, EBI-13885;
CC -!- MISCELLANEOUS: Present with 43500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000305}.
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DR EMBL; M57886; AAA34905.1; -; Genomic_DNA.
DR EMBL; X57338; CAA40614.1; -; Genomic_DNA.
DR EMBL; U18778; AAB64556.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07676.1; -; Genomic_DNA.
DR PIR; S25293; S25293.
DR RefSeq; NP_010940.3; NM_001178914.3.
DR AlphaFoldDB; P32263; -.
DR SMR; P32263; -.
DR BioGRID; 36757; 55.
DR DIP; DIP-1529N; -.
DR IntAct; P32263; 11.
DR MINT; P32263; -.
DR STRING; 4932.YER023W; -.
DR iPTMnet; P32263; -.
DR MaxQB; P32263; -.
DR PaxDb; P32263; -.
DR PRIDE; P32263; -.
DR EnsemblFungi; YER023W_mRNA; YER023W; YER023W.
DR GeneID; 856744; -.
DR KEGG; sce:YER023W; -.
DR SGD; S000000825; PRO3.
DR VEuPathDB; FungiDB:YER023W; -.
DR eggNOG; KOG3124; Eukaryota.
DR GeneTree; ENSGT00950000183044; -.
DR HOGENOM; CLU_042344_1_2_1; -.
DR InParanoid; P32263; -.
DR OMA; EQICTPK; -.
DR BioCyc; MetaCyc:YER023W-MON; -.
DR BioCyc; YEAST:YER023W-MON; -.
DR Reactome; R-SCE-8964539; Glutamate and glutamine metabolism.
DR UniPathway; UPA00098; UER00361.
DR PRO; PR:P32263; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32263; protein.
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; IMP:SGD.
DR GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
DR GO; GO:0006561; P:proline biosynthetic process; IMP:SGD.
DR HAMAP; MF_01925; P5C_reductase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR029036; P5CR_dimer.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR PANTHER; PTHR11645; PTHR11645; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00112; proC; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Isopeptide bond; NADP; Oxidoreductase;
KW Phosphoprotein; Proline biosynthesis; Reference proteome; Ubl conjugation.
FT CHAIN 1..286
FT /note="Pyrroline-5-carboxylate reductase"
FT /id="PRO_0000187328"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
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
