ID CITX_ECOLC Reviewed; 183 AA. AC B1IYJ2; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 29-APR-2008, sequence version 1. DT 16-JUN-2009, entry version 9. 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=EcolC_3030; OS Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=481805; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., RA Tice H., Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Ingram L., Richardson P.; RT "Complete sequence of Escherichia coli C str. ATCC 8739."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. 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; CP000946; ACA78654.1; -; Genomic_DNA. DR RefSeq; YP_001725981.1; -. DR GeneID; 6065423; -. DR GenomeReviews; CP000946_GR; EcolC_3030. DR KEGG; ecl:EcolC_3030; -. DR OMA; B1IYJ2; TGYEYYL. 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_1000080329. SQ SEQUENCE 183 AA; 20286 MW; 22B3643BDABE06C8 CRC64; MHLLPELASH HAVSIPELLV SRDERQARQH VWLKRHPVPL VSFTVVAPGP IKDCEVTRRI FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL WDIDVLTPEG EILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC NVN //