(data stored in SCRATCH zone)

SWISSPROT: C8U2Y0_ECO10

ID   C8U2Y0_ECO10            Unreviewed;        98 AA.
AC   C8U2Y0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=Citrate lyase acyl carrier protein {ECO:0000256|HAMAP-Rule:MF_00805};
DE   AltName: Full=Citrate lyase gamma chain {ECO:0000256|HAMAP-Rule:MF_00805};
GN   Name=citD {ECO:0000256|HAMAP-Rule:MF_00805,
GN   ECO:0000313|EMBL:BAI29488.1};
GN   OrderedLocusNames=ECO103_0625 {ECO:0000313|EMBL:BAI29488.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29488.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29488.1, 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: Covalent carrier of the coenzyme of citrate lyase.
CC       {ECO:0000256|HAMAP-Rule:MF_00805, ECO:0000256|SAAS:SAAS00343638}.
CC   -!- SUBUNIT: Oligomer with a subunit composition of (alpha,beta,
CC       gamma)6. {ECO:0000256|HAMAP-Rule:MF_00805,
CC       ECO:0000256|SAAS:SAAS00343634}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00805,
CC       ECO:0000256|SAAS:SAAS00343633}.
CC   -!- SIMILARITY: Belongs to the CitD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00805, ECO:0000256|SAAS:SAAS00539639}.
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DR   EMBL; AP010958; BAI29488.1; -; Genomic_DNA.
DR   RefSeq; WP_000700703.1; NC_013353.1.
DR   EnsemblBacteria; BAI29488; BAI29488; ECO103_0625.
DR   KEGG; eoh:ECO103_0625; -.
DR   HOGENOM; HOG000040480; -.
DR   KO; K01646; -.
DR   OMA; YNWKEID; -.
DR   BioCyc; ECOL585395:ECO103_RS03260-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   HAMAP; MF_00805; CitD; 1.
DR   InterPro; IPR006495; CitD.
DR   InterPro; IPR023439; Mal_deCO2ase/Cit_lyase_ACP.
DR   Pfam; PF06857; ACP; 1.
DR   PIRSF; PIRSF002736; Citrt_lyas_gamma; 1.
DR   ProDom; PD015389; CitD; 1.
DR   TIGRFAMs; TIGR01608; citD; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2Y0.
DR   SWISS-2DPAGE; C8U2Y0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00805,
KW   ECO:0000256|SAAS:SAAS00012626}; Lyase {ECO:0000313|EMBL:BAI29488.1};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_00805,
KW   ECO:0000256|PIRSR:PIRSR002736-50}.
FT   MOD_RES      14     14       O-(phosphoribosyl dephospho-coenzyme
FT                                A)serine. {ECO:0000256|HAMAP-Rule:
FT                                MF_00805, ECO:0000256|PIRSR:PIRSR002736-
FT                                50}.
SQ   SEQUENCE   98 AA;  10689 MW;  5932A2109978398A CRC64;
     MKINQPAVAG TLESGDVMIR IAPLDTQDID LQINSSVEKQ FGDAIRTTIL DVLARYNVRG
     VQLNVDDKGA LDCILRARLE ALLARASGIP ALPWEDCQ
//

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