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B6I0S3

- CITX_ECOSE

UniProt

B6I0S3 - CITX_ECOSE

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Protein

Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase

Gene

citX

Organism
Escherichia coli (strain SE11)
Status
Reviewed - 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-EC

GO - Biological processi

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

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Enzyme and pathway databases

BioCyciECOL409438:GHUU-691-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:ECSE_0682
OrganismiEscherichia coli (strain SE11)
Taxonomic identifieri409438 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000008199: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 183183Apo-citrate lyase phosphoribosyl-dephospho-CoA transferasePRO_1000189599Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi409438.ECSE_0682.

Structurei

3D structure databases

ProteinModelPortaliB6I0S3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CitX family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3697.
HOGENOMiHOG000130710.
KOiK05964.
OMAiQTFWLAT.
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.

B6I0S3-1 [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:December 16, 2008 - v1
Checksum:i22BC3420DABE06D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009240 Genomic DNA. Translation: BAG76206.1.
RefSeqiYP_002291957.1. NC_011415.1.

Genome annotation databases

EnsemblBacteriaiBAG76206; BAG76206; ECSE_0682.
GeneIDi6999053.
KEGGiecy:ECSE_0682.
PATRICi18419780. VBIEscCol83070_0806.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009240 Genomic DNA. Translation: BAG76206.1 .
RefSeqi YP_002291957.1. NC_011415.1.

3D structure databases

ProteinModelPortali B6I0S3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 409438.ECSE_0682.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAG76206 ; BAG76206 ; ECSE_0682 .
GeneIDi 6999053.
KEGGi ecy:ECSE_0682.
PATRICi 18419780. VBIEscCol83070_0806.

Phylogenomic databases

eggNOGi COG3697.
HOGENOMi HOG000130710.
KOi K05964.
OMAi QTFWLAT.
OrthoDBi EOG6T7NCD.

Enzyme and pathway databases

BioCyci ECOL409438:GHUU-691-MONOMER.

Family and domain databases

HAMAPi MF_00398. CitX.
InterProi IPR005551. CitX.
[Graphical view ]
Pfami PF03802. CitX. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR03124. citrate_citX. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Complete genome sequence and comparative analysis of the wild-type commensal Escherichia coli strain SE11 isolated from a healthy adult."
    Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H., Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.
    DNA Res. 15:375-386(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SE11.

Entry informationi

Entry nameiCITX_ECOSE
AccessioniPrimary (citable) accession number: B6I0S3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 16, 2008
Last modified: October 29, 2014
This is version 36 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