(data stored in ACNUC10821 zone)

SWISSPROT: C8U272_ECO10

ID   C8U272_ECO10            Unreviewed;       269 AA.
AC   C8U272;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 68.
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:BAI29230.1};
GN   OrderedLocusNames=ECO103_0361 {ECO:0000313|EMBL:BAI29230.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29230.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29230.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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; AP010958; BAI29230.1; -; Genomic_DNA.
DR   RefSeq; WP_001295331.1; NC_013353.1.
DR   SMR; C8U272; -.
DR   EnsemblBacteria; BAI29230; BAI29230; ECO103_0361.
DR   KEGG; eoh:ECO103_0361; -.
DR   HOGENOM; HOG000230247; -.
DR   KO; K00286; -.
DR   OMA; FYFIEAM; -.
DR   BioCyc; ECOL585395:ECO103_RS01890-MONOMER; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000000959; 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; C8U272.
DR   SWISS-2DPAGE; C8U272.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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;  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
//

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