(data stored in ACNUC7421 zone)

HOGENOM: ECOBR_1_PE572

ID   ECOBR_1_PE572                        STANDARD;      PRT;   183 AA.
AC   ECOBR_1_PE572; C6UCL7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Probable apo-citrate lyase phosphoribosyl-dephospho-CoA
DE   transferase; EC=2.7.7 61;AltName: Full=Apo-ACP
DE   nucleodityltransferase;AltName: Full=Holo-ACP synthase;AltName:
DE   Full=Holo-citrate lyase synthase; (ECOBR_1.PE572).
GN   Name=citX; OrderedLocusNames=ECB_00582;
OS   ESCHERICHIA COLI B STR. REL606.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=413997;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ECOBR_1.PE572.
CC       Escherichia coli B str. REL606 chromosome, complete genome.
CC       complete sequence.
CC   -!- ANNOTATIONS ORIGIN:C6UCL7_ECOBR
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   -!- GENE_FAMILY: HOG000130710 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; C6UCL7; -.
DR   EMBL; CP000819; ACT38267.1; -; Genomic_DNA.
DR   RefSeq; YP_003043803.1; NC_012967.1.
DR   ProteinModelPortal; C6UCL7; -.
DR   STRING; C6UCL7; -.
DR   EnsemblBacteria; EBESCT00000162705; EBESCP00000151453; EBESCG00000162765.
DR   GeneID; 8175453; -.
DR   GenomeReviews; CP000819_GR; ECB_00582.
DR   KEGG; ebr:ECB_00582; -.
DR   GeneTree; EBGT00050000009839; -.
DR   ProtClustDB; PRK01392; -.
DR   GO; GO:0050519; F:holo-citrate lyase synthase activity; IEA:HAMAP.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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.
DR   HOGENOMDNA; ECOBR_1.PE572; -.
KW   Complete proteome; Lyase; Nucleotidyltransferase; Transferase.
SQ   SEQUENCE   183 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MHLLPELASH HAVSIPELLV SRDERQARQH VWLKRHPVPL VSFTVVAPGP IKDSEVTRRI
     FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP ARDLKLATIE LEHSHPLGRL
     WDIDVLTPEG EILSRRDYSL PPRRCLLCEQ SAAVCARGKT HQLTDLLNRM EALLNDVDAC
     NVN
//

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