ID   P5CR_STAS1              Reviewed;         271 AA.
AC   Q49XV0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=SSP1250;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008934; BAE18395.1; -; Genomic_DNA.
DR   RefSeq; WP_011303054.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49XV0; -.
DR   SMR; Q49XV0; -.
DR   STRING; 342451.SSP1250; -.
DR   DNASU; 3616880; -.
DR   EnsemblBacteria; BAE18395; BAE18395; SSP1250.
DR   KEGG; ssp:SSP1250; -.
DR   eggNOG; COG0345; Bacteria.
DR   HOGENOM; CLU_042344_0_1_9; -.
DR   OMA; AKQTCLG; -.
DR   OrthoDB; 1349288at2; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000006371; Chromosome.
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; Reference proteome.
FT   CHAIN           1..271
FT                   /note="Pyrroline-5-carboxylate reductase"
FT                   /id="PRO_0000187307"
SQ   SEQUENCE   271 AA;  29870 MW;  A44EB03C234708DB CRC64;
     MKLVFYGAGN MAHAIFTGIV NSKVIDSNDI YLTNRSNEVA LKEYAEKLGV NYSYDDEALL
     KAADYVFLGT KPYDFESLAE RIKPFITDKN KFISIMAGLP ISYIREKLEA DNPIARIMPN
     TNAHVGHSVT GISFSSNFGP NSKDEVDELI NAFGSAIEVP EDNLHQVTAI TGSGPAFLYH
     VFEQYVTAGT RLGLEKAQVE ESIRNLIIGT SKMIERSELS MEQLRKNITS KGGTTQAGLN
     ALSQHDLESV FEDCLRAAVD RSVELSSQDE D