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Protein

2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthase

Gene

citG

Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA.UniRule annotation

Catalytic activityi

ATP + 3'-dephospho-CoA = 2'-(5-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + adenine.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciECOL585057:GJ8I-605-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthaseUniRule annotation (EC:2.4.2.52UniRule annotation)
Short name:
2-(5''-triphosphoribosyl)-3'-dephospho-CoA synthaseUniRule annotation
Gene namesi
Name:citGUniRule annotation
Ordered Locus Names:ECIAI39_0589
OrganismiEscherichia coli O7:K1 (strain IAI39 / ExPEC)
Taxonomic identifieri585057 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000749 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2922922-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A synthasePRO_1000123220Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliB7NLX3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CitG/MdcB family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000258582.
KOiK05966.
OMAiIHRGGIK.

Family and domain databases

HAMAPiMF_00397. CitG. 1 hit.
InterProiIPR002736. CitG.
IPR017551. TriPribosyl-deP-CoA_syn_CitG.
[Graphical view]
PfamiPF01874. CitG. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03125. citrate_citG. 1 hit.

Sequencei

Sequence statusi: Complete.

B7NLX3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMPATSTKT TKLATSLIDE YALLGWRAML TEVNLSPKPG LVDRINCGAH
60 70 80 90 100
KDMALEDFHR SALAIQGWLP RFIEFGACSA EMAPEAVLNG LRPIGMACEG
110 120 130 140 150
DMFRATAGVN THKGSIFSLG LLCAAIGRLL QLNQPVTPTT VCSTAASFCR
160 170 180 190 200
GLTDRELRTN NSQRTAGQRL YQQLGLTGAR GEAEAGYPLV INHALPHYLT
210 220 230 240 250
LLDQGLDPEL ALLDTLLLLM ATNGDTNVAS RGGEGGLRWL QREAQTLLNN
260 270 280 290
GGIRTPADLD YLRQFDRECI ERNLSPGGSA DLLILTWFLA QI
Length:292
Mass (Da):31,624
Last modified:February 10, 2009 - v1
Checksum:iC1A2C297F860DAD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928164 Genomic DNA. Translation: CAR16726.1.
RefSeqiWP_000062473.1. NC_011750.1.
YP_002406615.1. NC_011750.1.

Genome annotation databases

EnsemblBacteriaiCAR16726; CAR16726; ECIAI39_0589.
GeneIDi7150958.
KEGGiect:ECIAI39_0589.
PATRICi18329746. VBIEscCol51957_0626.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928164 Genomic DNA. Translation: CAR16726.1.
RefSeqiWP_000062473.1. NC_011750.1.
YP_002406615.1. NC_011750.1.

3D structure databases

ProteinModelPortaliB7NLX3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR16726; CAR16726; ECIAI39_0589.
GeneIDi7150958.
KEGGiect:ECIAI39_0589.
PATRICi18329746. VBIEscCol51957_0626.

Phylogenomic databases

HOGENOMiHOG000258582.
KOiK05966.
OMAiIHRGGIK.

Enzyme and pathway databases

BioCyciECOL585057:GJ8I-605-MONOMER.

Family and domain databases

HAMAPiMF_00397. CitG. 1 hit.
InterProiIPR002736. CitG.
IPR017551. TriPribosyl-deP-CoA_syn_CitG.
[Graphical view]
PfamiPF01874. CitG. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03125. citrate_citG. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCITG_ECO7I
AccessioniPrimary (citable) accession number: B7NLX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: September 7, 2016
This is version 48 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

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 one 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.