(data stored in ACNUC7421 zone)

SWISSPROT: CITX_SHISS

ID   CITX_SHISS              Reviewed;         183 AA.
AC   Q3Z4H9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 70.
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};
GN   OrderedLocusNames=SSON_0566;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ87333.1; -; Genomic_DNA.
DR   EnsemblBacteria; AAZ87333; AAZ87333; SSON_0566.
DR   KEGG; ssn:SSON_0566; -.
DR   HOGENOM; HOG000130710; -.
DR   KO; K05964; -.
DR   OMA; AFDIVIK; -.
DR   BioCyc; SSON300269:G1GL2-665-MONOMER; -.
DR   Proteomes; UP000002529; 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; Q3Z4H9.
DR   SWISS-2DPAGE; Q3Z4H9.
KW   Complete proteome; Nucleotidyltransferase; Transferase.
FT   CHAIN         1    183       Apo-citrate lyase phosphoribosyl-
FT                                dephospho-CoA transferase.
FT                                /FTId=PRO_1000049605.
SQ   SEQUENCE   183 AA;  20270 MW;  22BC3420DABE06D3 CRC64;
     MHLLPELASH HAVSIPELLV SRDERQARQH VWLKRHPVPL VSFTVVAPGP IKDSEVTRRI
     FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL
     WDIDVLTPEG EILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC
     NVN
//

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