(data stored in ACNUC7421 zone)

SWISSPROT: CITX_ECO27

ID   CITX_ECO27              Reviewed;         183 AA.
AC   B7UKQ6;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   05-DEC-2018, entry version 50.
DE   RecName: Full=Probable apo-citrate lyase phosphoribosyl-dephospho-CoA transferase {ECO:0000255|HAMAP-Rule:MF_00398};
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};
GN   OrderedLocusNames=E2348C_0515;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(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:0000255|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:0000255|HAMAP-Rule:MF_00398};
CC   -!- SIMILARITY: Belongs to the CitX family. {ECO:0000255|HAMAP-
CC       Rule:MF_00398}.
DR   EMBL; FM180568; CAS08063.1; -; Genomic_DNA.
DR   RefSeq; WP_000550407.1; NC_011601.1.
DR   PRIDE; B7UKQ6; -.
DR   EnsemblBacteria; CAS08063; CAS08063; E2348C_0515.
DR   KEGG; ecg:E2348C_0515; -.
DR   KO; K05964; -.
DR   OMA; AFDIVIK; -.
DR   BioCyc; ECOL574521:E2348C_RS02705-MONOMER; -.
DR   Proteomes; UP000008205; 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;
DR   PRODOM; B7UKQ6.
DR   SWISS-2DPAGE; B7UKQ6.
KW   Complete proteome; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    183       Probable apo-citrate lyase
FT                                phosphoribosyl-dephospho-CoA transferase.
FT                                /FTId=PRO_1000189601.
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
//

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