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Protein

Citrate synthase

Gene

gltA

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

Functioni

Catalytic activityi

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.PROSITE-ProRule annotation

Enzyme regulationi

Allosterically inhibited by NADH.

Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes isocitrate from oxaloacetate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase (gltA)
  2. 2-methylcitrate dehydratase (prpD), Aconitate hydratase B (acnB), Aconitate hydratase A (acnA), 2-methylcitrate synthase (prpC)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei306PROSITE-ProRule annotation1
Active sitei363PROSITE-ProRule annotation1

GO - Molecular functioni

  • citrate (Si)-synthase activity Source: InterPro
  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Tricarboxylic acid cycle

Enzyme and pathway databases

BioCyciEcoCyc:CITSYN-MONOMER.
ECOL316407:JW0710-MONOMER.
MetaCyc:CITSYN-MONOMER.
BRENDAi2.3.3.16. 2026.
SABIO-RKP0ABH7.
UniPathwayiUPA00223; UER00717.

Names & Taxonomyi

Protein namesi
Recommended name:
Citrate synthase (EC:2.3.3.16)
Gene namesi
Name:gltA
Synonyms:gluT, icdB
Ordered Locus Names:b0720, JW0710
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10402. gltA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi207C → S: Weakened NADH binding and inhibition. 1 Publication1
Mutagenesisi208E → A: Weakened NADH binding and inhibition. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001699431 – 427Citrate synthaseAdd BLAST427

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei283N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0ABH7.
PaxDbiP0ABH7.
PRIDEiP0ABH7.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-547808,EBI-547808
yegSP764072EBI-547808,EBI-1127478

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259941. 9 interactors.
DIPiDIP-36204N.
IntActiP0ABH7. 9 interactors.
MINTiMINT-1249502.
STRINGi511145.b0720.

Structurei

Secondary structure

1427
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Beta strandi8 – 18Combined sources11
Beta strandi24 – 26Combined sources3
Beta strandi29 – 31Combined sources3
Helixi35 – 38Combined sources4
Beta strandi47 – 61Combined sources15
Helixi62 – 64Combined sources3
Beta strandi66 – 69Combined sources4
Helixi74 – 80Combined sources7
Helixi83 – 92Combined sources10
Helixi98 – 110Combined sources13
Helixi116 – 122Combined sources7
Helixi131 – 139Combined sources9
Helixi140 – 144Combined sources5
Helixi147 – 149Combined sources3
Beta strandi152 – 154Combined sources3
Helixi155 – 181Combined sources27
Beta strandi190 – 192Combined sources3
Helixi194 – 203Combined sources10
Beta strandi206 – 208Combined sources3
Helixi214 – 225Combined sources12
Helixi234 – 244Combined sources11
Helixi249 – 261Combined sources13
Turni262 – 265Combined sources4
Helixi268 – 278Combined sources11
Beta strandi281 – 284Combined sources4
Turni285 – 288Combined sources4
Helixi290 – 292Combined sources3
Helixi300 – 302Combined sources3
Helixi316 – 329Combined sources14
Helixi331 – 333Combined sources3
Turni335 – 338Combined sources4
Helixi339 – 349Combined sources11
Helixi351 – 356Combined sources6
Helixi362 – 372Combined sources11
Helixi379 – 403Combined sources25
Beta strandi410 – 413Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NXEX-ray2.30A/B1-427[»]
1NXGX-ray2.50A/B1-427[»]
1OWBX-ray2.20A/B1-427[»]
1OWCX-ray2.20A/B1-427[»]
4G6BX-ray2.20A/B2-427[»]
4JADX-ray1.90A/B2-427[»]
4JAEX-ray2.70A/B2-427[»]
4JAFX-ray2.30A/B2-427[»]
4JAGX-ray2.10A/B2-427[»]
ProteinModelPortaliP0ABH7.
SMRiP0ABH7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABH7.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiENOG4105BZN. Bacteria.
COG0372. LUCA.
HOGENOMiHOG000021224.
InParanoidiP0ABH7.
KOiK01647.
OMAiNKEDGVR.
PhylomeDBiP0ABH7.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
IPR010953. Citrate_synthase_typ-I.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01798. cit_synth_I. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABH7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADTKAKLTL NGDTAVELDV LKGTLGQDVI DIRTLGSKGV FTFDPGFTST
60 70 80 90 100
ASCESKITFI DGDEGILLHR GFPIDQLATD SNYLEVCYIL LNGEKPTQEQ
110 120 130 140 150
YDEFKTTVTR HTMIHEQITR LFHAFRRDSH PMAVMCGITG ALAAFYHDSL
160 170 180 190 200
DVNNPRHREI AAFRLLSKMP TMAAMCYKYS IGQPFVYPRN DLSYAGNFLN
210 220 230 240 250
MMFSTPCEPY EVNPILERAM DRILILHADH EQNASTSTVR TAGSSGANPF
260 270 280 290 300
ACIAAGIASL WGPAHGGANE AALKMLEEIS SVKHIPEFVR RAKDKNDSFR
310 320 330 340 350
LMGFGHRVYK NYDPRATVMR ETCHEVLKEL GTKDDLLEVA MELENIALND
360 370 380 390 400
PYFIEKKLYP NVDFYSGIIL KAMGIPSSMF TVIFAMARTV GWIAHWSEMH
410 420
SDGMKIARPR QLYTGYEKRD FKSDIKR
Length:427
Mass (Da):48,015
Last modified:October 25, 2005 - v1
Checksum:iF30A9DBF1FC590D5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti11N → D AA sequence (PubMed:6380576).Curated1
Sequence conflicti289V → F in AAA23892 (Ref. 1) Curated1
Sequence conflicti289V → F AA sequence (PubMed:6380576).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01619 Genomic DNA. Translation: AAA23892.1.
U00096 Genomic DNA. Translation: AAC73814.1.
AP009048 Genomic DNA. Translation: BAA35384.1.
X00980 Genomic DNA. Translation: CAA25484.1.
V01501 Genomic DNA. Translation: CAA24746.1.
M28987 Genomic DNA. Translation: AAA23901.1.
M29373 Genomic DNA. Translation: AAA23902.1.
PIRiG64807. YKEC.
RefSeqiNP_415248.1. NC_000913.3.
WP_000785834.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73814; AAC73814; b0720.
BAA35384; BAA35384; BAA35384.
GeneIDi945323.
KEGGiecj:JW0710.
eco:b0720.
PATRICi32116635. VBIEscCol129921_0750.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01619 Genomic DNA. Translation: AAA23892.1.
U00096 Genomic DNA. Translation: AAC73814.1.
AP009048 Genomic DNA. Translation: BAA35384.1.
X00980 Genomic DNA. Translation: CAA25484.1.
V01501 Genomic DNA. Translation: CAA24746.1.
M28987 Genomic DNA. Translation: AAA23901.1.
M29373 Genomic DNA. Translation: AAA23902.1.
PIRiG64807. YKEC.
RefSeqiNP_415248.1. NC_000913.3.
WP_000785834.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NXEX-ray2.30A/B1-427[»]
1NXGX-ray2.50A/B1-427[»]
1OWBX-ray2.20A/B1-427[»]
1OWCX-ray2.20A/B1-427[»]
4G6BX-ray2.20A/B2-427[»]
4JADX-ray1.90A/B2-427[»]
4JAEX-ray2.70A/B2-427[»]
4JAFX-ray2.30A/B2-427[»]
4JAGX-ray2.10A/B2-427[»]
ProteinModelPortaliP0ABH7.
SMRiP0ABH7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259941. 9 interactors.
DIPiDIP-36204N.
IntActiP0ABH7. 9 interactors.
MINTiMINT-1249502.
STRINGi511145.b0720.

Proteomic databases

EPDiP0ABH7.
PaxDbiP0ABH7.
PRIDEiP0ABH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73814; AAC73814; b0720.
BAA35384; BAA35384; BAA35384.
GeneIDi945323.
KEGGiecj:JW0710.
eco:b0720.
PATRICi32116635. VBIEscCol129921_0750.

Organism-specific databases

EchoBASEiEB0397.
EcoGeneiEG10402. gltA.

Phylogenomic databases

eggNOGiENOG4105BZN. Bacteria.
COG0372. LUCA.
HOGENOMiHOG000021224.
InParanoidiP0ABH7.
KOiK01647.
OMAiNKEDGVR.
PhylomeDBiP0ABH7.

Enzyme and pathway databases

UniPathwayiUPA00223; UER00717.
BioCyciEcoCyc:CITSYN-MONOMER.
ECOL316407:JW0710-MONOMER.
MetaCyc:CITSYN-MONOMER.
BRENDAi2.3.3.16. 2026.
SABIO-RKP0ABH7.

Miscellaneous databases

EvolutionaryTraceiP0ABH7.
PROiP0ABH7.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR019810. Citrate_synthase_AS.
IPR024176. Citrate_synthase_bac-typ.
IPR010953. Citrate_synthase_typ-I.
[Graphical view]
PANTHERiPTHR11739. PTHR11739. 1 hit.
PfamiPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFiPIRSF001369. Citrate_synth. 1 hit.
PRINTSiPR00143. CITRTSNTHASE.
SUPFAMiSSF48256. SSF48256. 1 hit.
TIGRFAMsiTIGR01798. cit_synth_I. 1 hit.
PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCISY_ECOLI
AccessioniPrimary (citable) accession number: P0ABH7
Secondary accession number(s): O32552, P00891, P78257
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2005
Last modified: November 2, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.