(data stored in SCRATCH zone)

SWISSPROT: P5CR2_BACSU

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   11-DEC-2019, entry version 133.
DE   RecName: Full=Pyrroline-5-carboxylate reductase 2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE            Short=P5C reductase 2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE            Short=P5CR 2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE            EC=1.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01925};
DE   AltName: Full=PCA reductase 2 {ECO:0000255|HAMAP-Rule:MF_01925};
GN   Name=proI; Synonyms=yqjO; OrderedLocusNames=BSU23800;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
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 the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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, PATHWAY, AND DISRUPTION PHENOTYPE.
RX   PubMed=11418582; 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   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC       L-proline. {ECO:0000305|PubMed:11418582}.
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, ECO:0000269|PubMed:11418582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925}.
CC   -!- DISRUPTION PHENOTYPE: The proG proH proI triple mutant is auxotrophic
CC       for proline. {ECO:0000269|PubMed:11418582}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01925}.
DR   EMBL; D84432; BAA12621.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14312.1; -; Genomic_DNA.
DR   PIR; G69964; G69964.
DR   RefSeq; NP_390261.1; NC_000964.3.
DR   RefSeq; WP_004398788.1; NZ_JNCM01000036.1.
DR   SMR; P54552; -.
DR   STRING; 224308.BSU23800; -.
DR   PaxDb; P54552; -.
DR   PRIDE; P54552; -.
DR   EnsemblBacteria; CAB14312; CAB14312; BSU23800.
DR   GeneID; 938697; -.
DR   KEGG; bsu:BSU23800; -.
DR   PATRIC; fig|224308.179.peg.2593; -.
DR   eggNOG; ENOG4105II7; Bacteria.
DR   eggNOG; COG0345; LUCA.
DR   HOGENOM; HOG000230247; -.
DR   InParanoid; P54552; -.
DR   KO; K00286; -.
DR   OMA; AKMLQQE; -.
DR   PhylomeDB; P54552; -.
DR   BioCyc; BSUB:BSU23800-MONOMER; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IBA:GO_Central.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IBA:GO_Central.
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   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.
DR   PROSITE; PS00521; P5CR; 1.
PE   3: Inferred from homology;
DR   PRODOM; P54552.
DR   SWISS-2DPAGE; P54552.
KW   Amino-acid biosynthesis; Cytoplasm; NADP; Oxidoreductase;
KW   Proline biosynthesis; Reference proteome.
FT   CHAIN           1..278
FT                   /note="Pyrroline-5-carboxylate reductase 2"
FT                   /id="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
//

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