(data stored in SCRATCH zone)

SWISSPROT: Q8XEB1_ECO57

ID   Q8XEB1_ECO57            Unreviewed;       269 AA.
AC   Q8XEB1; Q7AH26;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   30-AUG-2017, entry version 119.
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:AAG54732.1};
GN   OrderedLocusNames=ECs0437 {ECO:0000313|EMBL:BAB33859.1}, Z0482
GN   {ECO:0000313|EMBL:AAG54732.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|Proteomes:UP000002519};
RN   [1] {ECO:0000313|EMBL:BAB33859.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558}, and Sakai
RC   {ECO:0000313|EMBL:BAB33859.1};
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [2] {ECO:0000313|EMBL:AAG54732.1, ECO:0000313|Proteomes:UP000002519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EDL933 {ECO:0000313|EMBL:AAG54732.1}, and O157:H7 / EDL933 /
RC   ATCC 700927 / EHEC {ECO:0000313|Proteomes:UP000002519};
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G.III., Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
CC   -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate
CC       (PCA) to L-proline. {ECO:0000256|HAMAP-Rule:MF_01925}.
CC   -!- CATALYTIC ACTIVITY: L-proline + NAD(P)(+) = 1-pyrroline-5-
CC       carboxylate + NAD(P)H. {ECO:0000256|HAMAP-Rule:MF_01925,
CC       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; AE005174; AAG54732.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33859.1; -; Genomic_DNA.
DR   PIR; D90683; D90683.
DR   PIR; H85533; H85533.
DR   RefSeq; NP_308463.1; NC_002695.1.
DR   RefSeq; WP_001301911.1; NZ_MWVM01000009.1.
DR   STRING; 155864.Z0482; -.
DR   EnsemblBacteria; AAG54732; AAG54732; Z0482.
DR   EnsemblBacteria; BAB33859; BAB33859; BAB33859.
DR   GeneID; 914538; -.
DR   KEGG; ece:Z0482; -.
DR   KEGG; ecs:ECs0437; -.
DR   PATRIC; fig|386585.9.peg.532; -.
DR   eggNOG; ENOG4105II7; Bacteria.
DR   eggNOG; COG0345; LUCA.
DR   HOGENOM; HOG000230247; -.
DR   KO; K00286; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-HAMAP.
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_C-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR028939; P5C_Rdtase_cat_N.
DR   InterPro; IPR029036; P5CR_dimer.
DR   InterPro; IPR000304; Pyrroline-COOH_reductase.
DR   PANTHER; PTHR11645; PTHR11645; 1.
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; Q8XEB1.
DR   SWISS-2DPAGE; Q8XEB1.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW   ECO:0000256|RuleBase:RU003903};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558,
KW   ECO:0000313|Proteomes:UP000002519};
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;  B28F9806069C1E32 CRC64;
     MEKKIGFIGC GNMGKAILGG LIASGQVLPG QIWVYTPSPD KVAALHDKFG 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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