Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase

Gene

citX

Organism
Shigella flexneri serotype 5b (strain 8401)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Transfers 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A on a serine residue to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield holo-acyl carrier protein.UniRule annotation

Catalytic activityi

2'-(5-triphosphoribosyl)-3'-dephospho-CoA + citrate lyase apo-[acyl-carrier protein] = citrate lyase holo-[acyl-carrier protein] + diphosphate.UniRule annotation

GO - Molecular functioni

  1. holo-citrate lyase synthase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. prosthetic group biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Enzyme and pathway databases

BioCyciSFLE373384:GHZM-566-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase (EC:2.7.7.61UniRule annotation)
Alternative name(s):
Apo-ACP nucleodityltransferaseUniRule annotation
Holo-ACP synthaseUniRule annotation
Holo-citrate lyase synthaseUniRule annotation
Gene namesi
Name:citXUniRule annotation
Ordered Locus Names:SFV_0567
OrganismiShigella flexneri serotype 5b (strain 8401)
Taxonomic identifieri373384 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000000659: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Apo-citrate lyase phosphoribosyl-dephospho-CoA transferasePRO_1000049604Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi373384.SFV_0567.

Family & Domainsi

Sequence similaritiesi

Belongs to the CitX family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3697.
HOGENOMiHOG000130710.
KOiK05964.
OMAiAFDIVIK.
OrthoDBiEOG6T7NCD.

Family and domain databases

HAMAPiMF_00398. CitX.
InterProiIPR005551. CitX.
[Graphical view]
PfamiPF03802. CitX. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03124. citrate_citX. 1 hit.

Sequencei

Sequence statusi: Complete.

Q0T702-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLLPELASH HAVSIPELLV SRDERQARQH AWLKHHPVPL VSFTVVAPGP
60 70 80 90 100
IKDSEVTRRI FNHRVTALRA LATKQGWQIQ EQAALVSASG PEGMLSIAAP
110 120 130 140 150
ARDLKLATIE LEHSHPLGRL WDIDVLTPEG EILSRRDYSL PPRRCLLCEQ
160 170 180
SAAVCARGKT HQLTDLLNRM EALLNDVDAC NVN
Length:183
Mass (Da):20,352
Last modified:September 5, 2006 - v1
Checksum:iCE28B0E0167A7B66
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000266 Genomic DNA. Translation: ABF02824.1.
RefSeqiYP_688129.1. NC_008258.1.

Genome annotation databases

EnsemblBacteriaiABF02824; ABF02824; SFV_0567.
GeneIDi4210651.
KEGGisfv:SFV_0567.
PATRICi18724209. VBIShiFle33408_0649.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000266 Genomic DNA. Translation: ABF02824.1.
RefSeqiYP_688129.1. NC_008258.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi373384.SFV_0567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABF02824; ABF02824; SFV_0567.
GeneIDi4210651.
KEGGisfv:SFV_0567.
PATRICi18724209. VBIShiFle33408_0649.

Phylogenomic databases

eggNOGiCOG3697.
HOGENOMiHOG000130710.
KOiK05964.
OMAiAFDIVIK.
OrthoDBiEOG6T7NCD.

Enzyme and pathway databases

BioCyciSFLE373384:GHZM-566-MONOMER.

Family and domain databases

HAMAPiMF_00398. CitX.
InterProiIPR005551. CitX.
[Graphical view]
PfamiPF03802. CitX. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03124. citrate_citX. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete genome sequence of Shigella flexneri 5b and comparison with Shigella flexneri 2a."
    Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.
    BMC Genomics 7:173-173(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 8401.

Entry informationi

Entry nameiCITX_SHIF8
AccessioniPrimary (citable) accession number: Q0T702
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: February 4, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.