ID   P5CR_STAAS              Reviewed;         271 AA.
AC   Q6G961;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE            Short=P5C reductase {ECO:0000255|HAMAP-Rule:MF_01925};
DE            Short=P5CR {ECO:0000255|HAMAP-Rule:MF_01925};
DE            EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE   AltName: Full=PCA reductase {ECO:0000255|HAMAP-Rule:MF_01925};
GN   Name=proC {ECO:0000255|HAMAP-Rule:MF_01925}; OrderedLocusNames=SAS1443;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC       L-proline. {ECO:0000255|HAMAP-Rule:MF_01925}.
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:0000255|HAMAP-Rule:MF_01925};
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:0000255|HAMAP-Rule:MF_01925};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC       from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_01925}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01925}.
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DR   EMBL; BX571857; CAG43220.1; -; Genomic_DNA.
DR   RefSeq; WP_000779749.1; NC_002953.3.
DR   AlphaFoldDB; Q6G961; -.
DR   SMR; Q6G961; -.
DR   PRIDE; Q6G961; -.
DR   KEGG; sas:SAS1443; -.
DR   HOGENOM; CLU_042344_0_1_9; -.
DR   OMA; AKQTCLG; -.
DR   UniPathway; UPA00098; UER00361.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis.
FT   CHAIN           1..271
FT                   /note="Pyrroline-5-carboxylate reductase"
FT                   /id="PRO_0000187302"
SQ   SEQUENCE   271 AA;  29826 MW;  BBFB9C15896A9633 CRC64;
     MKLVFYGAGN MAQAIFTGII NSSNLDANDI YLTNKSNEQA LKAFAEKLGV NYSYDDATLL
     KDADYVFLGT KPHDFDALAT RIKPHITKDN CFISIMAGIP IDYIKQQLEC QNPVARIMPN
     TNAQVGHSVT GISFSNNFDP KSKDEINDLV KAFGSVIEVS EDHLHQVTAI TGSGPAFLYH
     VFEQYVKAGT KLGLEKEQVE ESIRNLIIGT SKMIERSDLS MAQLRKNITS KGGTTQAGLD
     TLSQYDLVSI FEDCLNAAVD RSIELSNVED Q