(data stored in SCRATCH zone)

SWISSPROT: B7UJL0_ECO27

ID   B7UJL0_ECO27            Unreviewed;       269 AA.
AC   B7UJL0;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 69.
DE   RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
DE            Short=P5C reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE            Short=P5CR {ECO:0000256|HAMAP-Rule:MF_01925};
DE            EC=1.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
DE   AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925};
GN   Name=proC {ECO:0000256|HAMAP-Rule:MF_01925,
GN   ECO:0000313|EMBL:CAS07870.1};
GN   OrderedLocusNames=E2348C_0322 {ECO:0000313|EMBL:CAS07870.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07870.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07870.1, ECO:0000313|Proteomes:UP000008205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate
CC       (PCA) to L-proline. {ECO:0000256|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,
CC         ChEBI:CHEBI:15893, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:60039; EC=1.5.1.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01925};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+)
CC         + NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15893, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:60039; EC=1.5.1.2; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC       proline from L-glutamate 5-semialdehyde: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|RuleBase:RU003903}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}.
CC   -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase
CC       family. {ECO:0000256|HAMAP-Rule:MF_01925,
CC       ECO:0000256|RuleBase:RU003903}.
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DR   EMBL; FM180568; CAS07870.1; -; Genomic_DNA.
DR   RefSeq; WP_001339242.1; NC_011601.1.
DR   EnsemblBacteria; CAS07870; CAS07870; E2348C_0322.
DR   KEGG; ecg:E2348C_0322; -.
DR   HOGENOM; HOG000230247; -.
DR   KO; K00286; -.
DR   OMA; FYFIEAM; -.
DR   BioCyc; ECOL574521:E2348C_RS01695-MONOMER; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
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; B7UJL0.
DR   SWISS-2DPAGE; B7UJL0.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903}.
FT   DOMAIN        4     99       F420_oxidored. {ECO:0000259|Pfam:
FT                                PF03807}.
FT   DOMAIN      163    266       P5CR_dimer. {ECO:0000259|Pfam:PF14748}.
SQ   SEQUENCE   269 AA;  28203 MW;  1932C5EC4890F788 CRC64;
     MEKKIGFIGC GNMGKAILGG LIASGQVLPG QIWVYTPSPV KVTALHDQFG INAAESAQEV
     AQIADIIFAA VKPGIMIKVL SEITSSLNKD SLVVSIAAGI TLDQLARALG HDRKIIRAMP
     NTPALVNAGM TSVTPNALVT PEDTADVLNI FRCFGEAEVI AEPMIHPVVG VSGSSPAYVF
     MFIEAMADAA VLGGMPRAQA YKFAAQAVMG SAKMVLETGE HPGTLKDMVC SPGGTTIEAV
     RVLEEKGFRA AVIEAMTKCM EKSEKLSKS
//

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