ID CITX_ECOL5 Reviewed; 183 AA. AC Q0TK58; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 18. DE RecName: Full=Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase; DE EC=2.7.7.61; DE AltName: Full=Holo-ACP synthase; DE AltName: Full=Holo-citrate lyase synthase; DE AltName: Full=Apo-ACP nucleodityltransferase; GN Name=citX; OrderedLocusNames=ECP_0645; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). 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 (By similarity). CC -!- CATALYTIC ACTIVITY: 2'-(5-triphosphoribosyl)-3'-dephospho-CoA + CC citrate lyase apo-[acyl-carrier-protein] = citrate lyase holo- CC [acyl-carrier-protein] + diphosphate. CC -!- SIMILARITY: Belongs to the citX family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000247; ABG68673.1; -; Genomic_DNA. DR RefSeq; YP_668572.1; -. DR GeneID; 4188202; -. DR GenomeReviews; CP000247_GR; ECP_0645. DR KEGG; ecp:ECP_0645; -. DR HOGENOM; Q0TK58; -. DR OMA; Q0TK58; TGYEYYL. DR BioCyc; ECOL362663:ECP_0645-MON; -. DR GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:HAMAP. DR HAMAP; MF_00398; -; 1. DR InterPro; IPR005551; CitX. DR Pfam; PF03802; CitX; 1. DR TIGRFAMs; TIGR03124; ctirate_citX; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotidyltransferase; Transferase. FT CHAIN 1 183 Apo-citrate lyase phosphoribosyl- FT dephospho-CoA transferase. FT /FTId=PRO_1000049602. SQ SEQUENCE 183 AA; 20228 MW; 353DAB41BC78CBCE CRC64; MHLLPELASH HAVSIPELLV SRDERQARQH AWLKRHPVPL VSFTVVAPGP IKDSEVTRRI FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL WDIDVLTPEG DILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC NVN //