ID   P5CR_SHIFL              Reviewed;         269 AA.
AC   P0A9L9; P00373;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Pyrroline-5-carboxylate reductase;
DE            Short=P5C reductase;
DE            Short=P5CR;
DE            EC=1.5.1.2;
GN   Name=proC; OrderedLocusNames=SF0322, S0330;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   MEDLINE=22590274; PubMed=12704152;
RX   DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN41981.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP15859.1; -; Genomic_DNA.
DR   RefSeq; NP_706274.1; -.
DR   RefSeq; NP_836053.1; -.
DR   GeneID; 1027435; -.
DR   GeneID; 1076763; -.
DR   GenomeReviews; AE005674_GR; SF0322.
DR   GenomeReviews; AE014073_GR; S0330.
DR   KEGG; sfl:SF0322; -.
DR   KEGG; sfx:S0330; -.
DR   HOGENOM; P0A9L9; -.
DR   OMA; P0A9L9; LKQGYPA.
DR   BioCyc; SFLE198214:AAN41981.1-MON; -.
DR   BRENDA; 1.5.1.2; 189495.
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; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR004455; NADP_OxRdtase_F420.
DR   InterPro; IPR000304; P5CR.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11645; P5CR; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 1.
DR   TIGRFAMs; TIGR00112; proC; 1.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Complete proteome; Cytoplasm; NADP;
KW   Oxidoreductase; Proline biosynthesis.
FT   CHAIN         1    269       Pyrroline-5-carboxylate reductase.
FT                                /FTId=PRO_0000187297.
SQ   SEQUENCE   269 AA;  28145 MW;  C5E2CED36BCC508D CRC64;
     MEKKIGFIGC GNMGKAILGG LIASGQVLPG QIWVYTPSPD KVAALHDQFG INAAESAQEV
     AQIADIIFAA VKPGIMIKVL SEITSSLNKD SLVVSIAAGV TLDQLARALG HDRKIIRAMP
     NTPALVNAGM TSVTPNALVT PEDTADVLNI FRCFGEAEVI AEPMIHPVVG VSGSSPAYVF
     MFIEAMADAA VLGGMPRAQA YKFAAQAVMG SAKMVLETGE HPGALKDMVC SPGGTTIEAV
     RVLEEKGFRA AVIEAMTKCM EKSEKLSKS
//