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

Probable apo-citrate lyase phosphoribosyl-dephospho-CoA transferase

Gene

citX

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Enzyme and pathway databases

BioCyciECOL595496:GI18-503-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable apo-citrate lyase phosphoribosyl-dephospho-CoA transferaseUniRule annotation (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:BWG_0487
OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
Taxonomic identifieri595496 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Probable apo-citrate lyase phosphoribosyl-dephospho-CoA transferasePRO_1000205876Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliC4ZWA3.
ModBaseiSearch...
MobiDBiSearch...

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.

C4ZWA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLLPELASH HAVSIPELLV SRDERQARQH VWLKRHPVPL VSFTVVAPGP
60 70 80 90 100
IKDSEVTRRI FNHGVTALRA LAAKQGWQIQ EQAALVSASG PEGMLSIAAP
110 120 130 140 150
ARDLKLATIE LEHSHPLGRL WDIDVLTPEG EILSRRDYSL PPRRCLLCEQ
160 170 180
SAAVCARGKT HQLTDLLNRM EALLNDVDAC NVN
Length:183
Mass (Da):20,270
Last modified:July 28, 2009 - v1
Checksum:i22BC3420DABE06D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR61998.1.
RefSeqiWP_000550422.1. NC_012759.1.
YP_002925689.1. NC_012759.1.

Genome annotation databases

EnsemblBacteriaiACR61998; ACR61998; BWG_0487.
KEGGiebw:BWG_0487.
PATRICi18269970. VBIEscCol60876_0540.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001396 Genomic DNA. Translation: ACR61998.1.
RefSeqiWP_000550422.1. NC_012759.1.
YP_002925689.1. NC_012759.1.

3D structure databases

ProteinModelPortaliC4ZWA3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACR61998; ACR61998; BWG_0487.
KEGGiebw:BWG_0487.
PATRICi18269970. VBIEscCol60876_0540.

Phylogenomic databases

eggNOGiCOG3697.
HOGENOMiHOG000130710.
KOiK05964.
OMAiAFDIVIK.
OrthoDBiEOG6T7NCD.

Enzyme and pathway databases

BioCyciECOL595496:GI18-503-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. "Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
    Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
    J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MC4100 / BW2952.

Entry informationi

Entry nameiCITX_ECOBW
AccessioniPrimary (citable) accession number: C4ZWA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: June 24, 2015
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.