(data stored in SCRATCH zone)

SWISSPROT: B7UJI2_ECO27

ID   B7UJI2_ECO27            Unreviewed;       389 AA.
AC   B7UJI2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 56.
DE   RecName: Full=Citrate synthase {ECO:0000256|PIRNR:PIRNR001369};
GN   Name=prpC {ECO:0000313|EMBL:CAS07840.1};
GN   OrderedLocusNames=E2348C_0292 {ECO:0000313|EMBL:CAS07840.1};
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS07840.1, ECO:0000313|Proteomes:UP000008205};
RN   [1] {ECO:0000313|EMBL:CAS07840.1, 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   -!- SIMILARITY: Belongs to the citrate synthase family.
CC       {ECO:0000256|PIRNR:PIRNR001369, ECO:0000256|RuleBase:RU003406}.
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DR   EMBL; FM180568; CAS07840.1; -; Genomic_DNA.
DR   RefSeq; WP_001285876.1; NC_011601.1.
DR   EnsemblBacteria; CAS07840; CAS07840; E2348C_0292.
DR   KEGG; ecg:E2348C_0292; -.
DR   HOGENOM; HOG000021225; -.
DR   KO; K01659; -.
DR   OMA; NFLWMTF; -.
DR   BioCyc; ECOL574521:E2348C_RS01540-MONOMER; -.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0046912; F:transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.10.230.10; -; 1.
DR   Gene3D; 1.10.580.10; -; 1.
DR   InterPro; IPR011278; 2-MeCitrate/Citrate_synth_II.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase.
DR   InterPro; IPR019810; Citrate_synthase_AS.
DR   InterPro; IPR024176; Citrate_synthase_bac-typ.
DR   InterPro; IPR036969; Citrate_synthase_sf.
DR   PANTHER; PTHR11739; PTHR11739; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PIRSF; PIRSF001369; Citrate_synth; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; SSF48256; 1.
DR   TIGRFAMs; TIGR01800; cit_synth_II; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; B7UJI2.
DR   SWISS-2DPAGE; B7UJI2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008205};
KW   Transferase {ECO:0000256|PIRNR:PIRNR001369,
KW   ECO:0000256|RuleBase:RU003406}.
FT   ACT_SITE    274    274       {ECO:0000256|PIRSR:PIRSR001369-1}.
FT   ACT_SITE    325    325       {ECO:0000256|PIRSR:PIRSR001369-1}.
SQ   SEQUENCE   389 AA;  43150 MW;  E237B66126EAEB20 CRC64;
     MSDTTILQNC THVIKPKKSV ALSGVPAGNT ALCTVGKSGN DLHYRGYDIL DLAEHCEFEE
     VAHLLIHGKL PTRDELAAYK TKLKALRGLP ANVRTVLEAL PAASHPMDVM RTGVSALGCT
     LPEKEGHTVS GARDIADKLL ASLSSILLYW YHYSHNGERI QPETDDDSIG GHFLHLLHGE
     KPSQSWEKAM HISLVLYAEH EFNASTFTSR VIAGTGSDMY SAIIGAIGAL RGPKHGGANE
     VSLEIQQRYE TPDEAEADIR KRVENKEVVI GFGHPVYTIA DPRHQVIKRV AKQLSQEGGS
     LKMYNIADRL ETVMWESKKM FPNLDWFSAV SYNMMGVPTE MFTPLFVIAR VTGWAAHIIE
     QRQDNKIIRP SANYVGPEDR QFVALDKRQ
//

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