ID   P5CR2_BACSU             Reviewed;         278 AA.
AC   P54552;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 62.
DE   RecName: Full=Pyrroline-5-carboxylate reductase 2;
DE            Short=P5C reductase 2;
DE            Short=P5CR 2;
DE            EC=1.5.1.2;
GN   Name=proI; Synonyms=yqjO; OrderedLocusNames=BSU23800;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   MEDLINE=97124195; PubMed=8969508;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of
RT   the Bacillus subtilis genome containing the skin element and many
RT   sporulation genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=21311767; PubMed=11418582;
RX   DOI=10.1128/JB.183.14.4389-4392.2001;
RA   Belitsky B.R., Brill J., Bremer E., Sonenshein A.L.;
RT   "Multiple genes for the last step of proline biosynthesis in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 183:4389-4392(2001).
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; D84432; BAA12621.1; -; Genomic_DNA.
DR   EMBL; Z99116; CAB14312.1; -; Genomic_DNA.
DR   PIR; G69964; G69964.
DR   RefSeq; NP_390261.1; -.
DR   GeneID; 938697; -.
DR   GenomeReviews; AL009126_GR; BSU23800.
DR   KEGG; bsu:BSU23800; -.
DR   NMPDR; fig|224308.1.peg.2385; -.
DR   SubtiList; BG11744; proI.
DR   HOGENOM; P54552; -.
DR   BioCyc; BSUB224308:BSU2379-MON; -.
DR   LinkHub; P54552; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
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.
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    278       Pyrroline-5-carboxylate reductase 2.
FT                                /FTId=PRO_0000187286.
SQ   SEQUENCE   278 AA;  30396 MW;  4B69DB527E55345E CRC64;
     MKKIGFVGAG SMAEAMINGI LQSGITKPEH IYITNRSNDE RLIELKETYS VRPCRDKNEF
     FTHTDIIILA FKPKDAAESI DSIRPYIKDQ LVISVLAGLT IETIQHYFGR KLAVIRVMPN
     TSAAIRKSAT GFSVSTEASK NDIIAAKALL ETIGDATLVE ERHLDAVTAI AGSGPAYVYR
     YIEAMEKAAQ KVGLDKETAK ALILQTMAGA TDMLLQSGKQ PEKLRKEITS PGGTTEAGLR
     ALQDSRFEEA IIHCIEETAK RSAEIKEQFA GAALERHS
//