(data stored in ACNUC10821 zone)

SWISSPROT: C8U2X7_ECO10

ID   C8U2X7_ECO10            Unreviewed;       183 AA.
AC   C8U2X7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 44.
DE   RecName: Full=Probable apo-citrate lyase phosphoribosyl-dephospho-CoA transferase {ECO:0000256|HAMAP-Rule:MF_00398};
DE            EC=2.7.7.61 {ECO:0000256|HAMAP-Rule:MF_00398};
DE   AltName: Full=Apo-ACP nucleodityltransferase {ECO:0000256|HAMAP-Rule:MF_00398};
DE   AltName: Full=Holo-ACP synthase {ECO:0000256|HAMAP-Rule:MF_00398};
DE   AltName: Full=Holo-citrate lyase synthase {ECO:0000256|HAMAP-Rule:MF_00398};
GN   Name=citX {ECO:0000256|HAMAP-Rule:MF_00398,
GN   ECO:0000313|EMBL:BAI29485.1};
GN   OrderedLocusNames=ECO103_0622 {ECO:0000313|EMBL:BAI29485.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29485.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29485.1, 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: Transfers 2-(5''-triphosphoribosyl)-3'-
CC       dephosphocoenzyme-A on a serine residue to the apo-acyl carrier
CC       protein (gamma chain) of the citrate lyase to yield holo-acyl
CC       carrier protein. {ECO:0000256|HAMAP-Rule:MF_00398}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA +
CC         apo-[citrate lyase ACP] = diphosphate + holo-[citrate lyase
CC         ACP]; Xref=Rhea:RHEA:16333, Rhea:RHEA-COMP:10157, Rhea:RHEA-
CC         COMP:10158, ChEBI:CHEBI:29999, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61378, ChEBI:CHEBI:82683; EC=2.7.7.61;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00398};
CC   -!- SIMILARITY: Belongs to the CitX family. {ECO:0000256|HAMAP-
CC       Rule:MF_00398}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010958; BAI29485.1; -; Genomic_DNA.
DR   RefSeq; WP_000550424.1; NC_013353.1.
DR   EnsemblBacteria; BAI29485; BAI29485; ECO103_0622.
DR   KEGG; eoh:ECO103_0622; -.
DR   HOGENOM; HOG000130710; -.
DR   KO; K05964; -.
DR   OMA; AFDIVIK; -.
DR   BioCyc; ECOL585395:ECO103_RS03245-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051191; P:prosthetic group biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_00398; CitX; 1.
DR   InterPro; IPR005551; CitX.
DR   Pfam; PF03802; CitX; 1.
DR   TIGRFAMs; TIGR03124; citrate_citX; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U2X7.
DR   SWISS-2DPAGE; C8U2X7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Lyase {ECO:0000313|EMBL:BAI29485.1};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00398};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00398,
KW   ECO:0000313|EMBL:BAI29485.1}.
SQ   SEQUENCE   183 AA;  20201 MW;  C3F92120DABE06D2 CRC64;
     MHLLPELASH HAVSIPELLV SRDERQARQH VWLKRHPVPL VSFTVVAPGP IKDSEVTRRI
     FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL
     WDIDVLTPEG EILSRRDYSL PPRSCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC
     NVN
//

If you have problems or comments...

PBIL Back to PBIL home page