ID   P5CR_STAHJ              Reviewed;         271 AA.
AC   Q4L6K3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=Pyrroline-5-carboxylate reductase;
DE            Short=P5C reductase;
DE            Short=P5CR;
DE            EC=1.5.1.2;
GN   Name=proC; OrderedLocusNames=SH1413;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA   Lee J.C., Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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; AP006716; BAE04722.1; -; Genomic_DNA.
DR   RefSeq; YP_253328.1; -.
DR   GeneID; 3483380; -.
DR   GenomeReviews; AP006716_GR; SH1413.
DR   KEGG; sha:SH1413; -.
DR   NMPDR; fig|279808.3.peg.1901; -.
DR   HOGENOM; Q4L6K3; -.
DR   OMA; Q4L6K3; FYFLEAM.
DR   BioCyc; SHAE279808:SH1413-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase; Proline biosynthesis.
FT   CHAIN         1    271       Pyrroline-5-carboxylate reductase.
FT                                /FTId=PRO_0000187306.
SQ   SEQUENCE   271 AA;  30168 MW;  90DAC8041979B794 CRC64;
     MKLVFYGAGN MAQAIFKGII NSKKLKSHDI YLTNKSNEEA LKNFAEELGV EYSYDDEKLL
     QDADYVFLGS KPYDFEKVAQ RIQPYINENN RFISIMAGLP INYIQEQLQV ENPIARIMPN
     TNAQVGHSVT GISFSGNFGP KSKEEVNDLV NAFGSVIEVD EDHLHQVTAI TGSGPAFLYH
     VFEQYVKAGT DLGLEKDQVE ESIKNLIIGT SKMIERSDLS MEQLRKNITS KGGTTQAGLN
     ALAQHDIEAI FKDCLNAAVH RSVELSKNED N
//