CITX_ECOHS
ID CITX_ECOHS Reviewed; 183 AA.
AC A7ZXP1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase;
DE EC=2.7.7.61 {ECO:0000255|HAMAP-Rule:MF_00398};
DE AltName: Full=Apo-ACP nucleodityltransferase {ECO:0000255|HAMAP-Rule:MF_00398};
DE AltName: Full=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00398};
DE AltName: Full=Holo-citrate lyase synthase {ECO:0000255|HAMAP-Rule:MF_00398};
GN Name=citX {ECO:0000255|HAMAP-Rule:MF_00398}; OrderedLocusNames=EcHS_A0665;
OS Escherichia coli O9:H4 (strain HS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
CC -!- FUNCTION: Transfers 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A on
CC a serine residue to the apo-acyl carrier protein (gamma chain) of the
CC citrate lyase to yield holo-acyl carrier protein. {ECO:0000255|HAMAP-
CC Rule:MF_00398}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-
CC [citrate lyase ACP] = diphosphate + holo-[citrate lyase ACP];
CC Xref=Rhea:RHEA:16333, Rhea:RHEA-COMP:10157, Rhea:RHEA-COMP:10158,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:33019, ChEBI:CHEBI:61378,
CC ChEBI:CHEBI:82683; EC=2.7.7.61; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00398};
CC -!- SIMILARITY: Belongs to the CitX family. {ECO:0000255|HAMAP-
CC Rule:MF_00398}.
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DR EMBL; CP000802; ABV05045.1; -; Genomic_DNA.
DR RefSeq; WP_000550414.1; NC_009800.1.
DR AlphaFoldDB; A7ZXP1; -.
DR SMR; A7ZXP1; -.
DR KEGG; ecx:EcHS_A0665; -.
DR HOGENOM; CLU_104529_1_1_6; -.
DR OMA; CGRSRKH; -.
DR Proteomes; UP000001123; Chromosome.
DR GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:UniProtKB-UniRule.
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;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..183
FT /note="Apo-citrate lyase phosphoribosyl-dephospho-CoA
FT transferase"
FT /id="PRO_1000060794"
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