ID   P5CR_STAAR              Reviewed;         271 AA.
AC   Q6GGJ5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Pyrroline-5-carboxylate reductase;
DE            Short=P5C reductase;
DE            Short=P5CR;
DE            EC=1.5.1.2;
GN   Name=proC; OrderedLocusNames=SAR1579;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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.
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DR   EMBL; BX571856; CAG40575.1; -; Genomic_DNA.
DR   RefSeq; YP_040977.1; -.
DR   GeneID; 2860829; -.
DR   GenomeReviews; BX571856_GR; SAR1579.
DR   KEGG; sar:SAR1579; -.
DR   HOGENOM; Q6GGJ5; -.
DR   OMA; Q6GGJ5; AMPNTSA.
DR   BioCyc; SAUR282458:SAR1579-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_0000187301.
SQ   SEQUENCE   271 AA;  29840 MW;  BBFB9C07196A9633 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 RSIELSNIED Q
//