(data stored in SCRATCH zone)

SWISSPROT: A0A0H3JCJ9_ECO57

ID   A0A0H3JCJ9_ECO57        Unreviewed;       307 AA.
AC   A0A0H3JCJ9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 15.
DE   SubName: Full=Citrate lyase beta chain {ECO:0000313|EMBL:BAB34078.1};
GN   OrderedLocusNames=ECs0655 {ECO:0000313|EMBL:BAB34078.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB34078.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB34078.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
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).
CC   -!- SIMILARITY: Belongs to the HpcH/HpaI aldolase family.
CC       {ECO:0000256|SAAS:SAAS00571010}.
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DR   EMBL; BA000007; BAB34078.1; -; Genomic_DNA.
DR   RefSeq; NP_308682.2; NC_002695.1.
DR   ProteinModelPortal; A0A0H3JCJ9; -.
DR   STRING; 155864.Z0760; -.
DR   EnsemblBacteria; BAB34078; BAB34078; BAB34078.
DR   GeneID; 917015; -.
DR   KEGG; ecs:ECs0655; -.
DR   PATRIC; fig|386585.9.peg.766; -.
DR   KO; K01644; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0009346; C:citrate lyase complex; IEA:InterPro.
DR   GO; GO:0008816; F:citryl-CoA lyase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro.
DR   InterPro; IPR005000; Aldolase/citrate-lyase_domain.
DR   InterPro; IPR011206; Citrate_lyase_beta/mcl1/mcl2.
DR   InterPro; IPR006475; Citrate_lyase_beta_bac.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   Pfam; PF03328; HpcH_HpaI; 1.
DR   PIRSF; PIRSF015582; Cit_lyase_B; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   TIGRFAMs; TIGR01588; citE; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H3JCJ9.
DR   SWISS-2DPAGE; A0A0H3JCJ9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000558};
KW   Lyase {ECO:0000313|EMBL:BAB34078.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR015582-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR015582-2,
KW   ECO:0000256|SAAS:SAAS00088067}.
FT   DOMAIN       20    239       HpcH_HpaI. {ECO:0000259|Pfam:PF03328}.
FT   METAL       144    144       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   METAL       171    171       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR015582-2}.
FT   BINDING      81     81       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
FT   BINDING     144    144       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR015582-1}.
SQ   SEQUENCE   307 AA;  33579 MW;  1D4985E4962A6B45 CRC64;
     MGGLPMISAS LQQRKTRTRR SMLFVPGANA AMVSNSFIYP ADALMFDLEE SVALREKDTA
     RRMVYHALQH PLYRDIETIV RVNALDSEWG VNDLEAVVRG GADVVRLPKT DTAQDVLDIE
     KEILRIEKAC GREPGSTGLL AAIESPLGIT RAVEIAHASE RLIGIALGAE DYVRNLRTER
     SPEGTELLFA RCSILQAARS AGIQAFDTVY SDANNEAGFL QEAAHIKQLG FDGKSLINPR
     QIDLLHNLYA PTQKEVDHAR RVVEAAEAAA REGLGVVSLN GKMVDGPVID RARLVLSRAE
     LSGIREE
//

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