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Protein

[Citrate [pro-3S]-lyase] ligase

Gene

citC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.

Catalytic activityi

ATP + acetate + [citrate (pro-3S)-lyase](thiol form) = AMP + diphosphate + [citrate (pro-3S)-lyase](acetyl form).

GO - Molecular functioni

  • [citrate (pro-3S)-lyase] ligase activity Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • N-acetyltransferase activity Source: InterPro

GO - Biological processi

  • biosynthetic process Source: InterPro
  • cellular protein modification process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CITC-MONOMER.
ECOL316407:JW0610-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
[Citrate [pro-3S]-lyase] ligase (EC:6.2.1.22)
Alternative name(s):
Acetate:SH-citrate lyase ligase
Citrate lyase synthetase
Gene namesi
Name:citC
Synonyms:ybeO
Ordered Locus Names:b0618, JW0610
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13645. citC.

Pathology & Biotechi

Chemistry

DrugBankiDB00336. Nitrofural.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352[Citrate [pro-3S]-lyase] ligasePRO_0000089770Add
BLAST

Proteomic databases

PaxDbiP77390.
PRIDEiP77390.

Expressioni

Inductioni

Repressed by H-NS. Part of the citCDEFXG operon.1 Publication

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
yaiIP0A8D32EBI-1119239,EBI-1116378

Protein-protein interaction databases

BioGridi4259904. 14 interactions.
IntActiP77390. 9 interactions.
STRINGi511145.b0618.

Structurei

3D structure databases

ProteinModelPortaliP77390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 128128N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105DUA. Bacteria.
COG3053. LUCA.
HOGENOMiHOG000117934.
InParanoidiP77390.
KOiK01910.
OMAiKGHQYLV.
PhylomeDBiP77390.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR005216. Citrate_lyase_ligase.
IPR013166. Citrate_lyase_ligase_C.
IPR004821. Cyt_trans-like.
IPR000182. GNAT_dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF08218. Citrate_ly_lig. 1 hit.
[Graphical view]
PIRSFiPIRSF005751. Acet_citr_lig. 1 hit.
SMARTiSM00764. Citrate_ly_lig. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR00124. cit_ly_ligase. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P77390-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGNDIFTRV KRSENKKMAE IAQFLHENDL SVDTTVEVFI TVTRDEKLIA
60 70 80 90 100
CGGIAGNIIK CVAISESVRG EGLALTLATE LINLAYERHS THLFIYTKTE
110 120 130 140 150
YEALFRQCGF STLTSVPGVM VLMENSATRL KRYAESLKKF RHPGNKIGCI
160 170 180 190 200
VMNANPFTNG HRYLIQQAAA QCDWLHLFLV KEDSSRFPYE DRLDLVLKGT
210 220 230 240 250
ADIPRLTVHR GSEYIISRAT FPCYFIKEQS VINHCYTEID LKIFRQYLAP
260 270 280 290 300
ALGVTHRFVG TEPFCRVTAQ YNQDMRYWLE TPTISAPPIE LVEIERLRYQ
310 320 330 340 350
EMPISASRVR QLLAKNDLTA IAPLVPAVTL HYLQNLLEHS RQDAAARQKT

PA
Length:352
Mass (Da):40,077
Last modified:November 1, 1997 - v2
Checksum:iF5894FFCD0F06518
GO

Sequence cautioni

The sequence AAB40818 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40818.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73719.2.
AP009048 Genomic DNA. Translation: BAA35254.2.
U46667 Genomic DNA. Translation: AAC28950.1.
PIRiH64795.
RefSeqiNP_415151.4. NC_000913.3.
WP_000467705.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73719; AAC73719; b0618.
BAA35254; BAA35254; BAA35254.
GeneIDi945231.
KEGGiecj:JW0610.
eco:b0618.
PATRICi32116416. VBIEscCol129921_0648.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82598 Genomic DNA. Translation: AAB40818.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73719.2.
AP009048 Genomic DNA. Translation: BAA35254.2.
U46667 Genomic DNA. Translation: AAC28950.1.
PIRiH64795.
RefSeqiNP_415151.4. NC_000913.3.
WP_000467705.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP77390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259904. 14 interactions.
IntActiP77390. 9 interactions.
STRINGi511145.b0618.

Chemistry

DrugBankiDB00336. Nitrofural.

Proteomic databases

PaxDbiP77390.
PRIDEiP77390.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73719; AAC73719; b0618.
BAA35254; BAA35254; BAA35254.
GeneIDi945231.
KEGGiecj:JW0610.
eco:b0618.
PATRICi32116416. VBIEscCol129921_0648.

Organism-specific databases

EchoBASEiEB3409.
EcoGeneiEG13645. citC.

Phylogenomic databases

eggNOGiENOG4105DUA. Bacteria.
COG3053. LUCA.
HOGENOMiHOG000117934.
InParanoidiP77390.
KOiK01910.
OMAiKGHQYLV.
PhylomeDBiP77390.

Enzyme and pathway databases

BioCyciEcoCyc:CITC-MONOMER.
ECOL316407:JW0610-MONOMER.

Miscellaneous databases

PROiP77390.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR005216. Citrate_lyase_ligase.
IPR013166. Citrate_lyase_ligase_C.
IPR004821. Cyt_trans-like.
IPR000182. GNAT_dom.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF08218. Citrate_ly_lig. 1 hit.
[Graphical view]
PIRSFiPIRSF005751. Acet_citr_lig. 1 hit.
SMARTiSM00764. Citrate_ly_lig. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
TIGRFAMsiTIGR00124. cit_ly_ligase. 1 hit.
TIGR00125. cyt_tran_rel. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCITC_ECOLI
AccessioniPrimary (citable) accession number: P77390
Secondary accession number(s): O54337, Q9R2T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: September 7, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.