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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei306 – 3061PROSITE-ProRule annotation
Active sitei363 – 3631PROSITE-ProRule annotation

GO - Molecular functioni

  1. citrate (Si)-synthase activity Source: InterPro
  2. identical protein binding Source: IntAct

GO - Biological processi

  1. cellular carbohydrate metabolic process Source: InterPro
  2. tricarboxylic acid cycle Source: UniProtKB-UniPathway
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.
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10402. gltA.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi207 – 2071C → S: Weakened NADH binding and inhibition. 1 Publication
Mutagenesisi208 – 2081E → A: Weakened NADH binding and inhibition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 427427Citrate synthasePRO_0000169943Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei283 – 2831N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0ABH7.
PRIDEiP0ABH7.

Expressioni

Gene expression databases

GenevestigatoriP0ABH7.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

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

Protein-protein interaction databases

DIPiDIP-36204N.
IntActiP0ABH7. 9 interactions.
MINTiMINT-1249502.
STRINGi511145.b0720.

Structurei

Secondary structure

1
427
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 64Combined sources
Beta strandi8 – 1811Combined sources
Beta strandi24 – 263Combined sources
Beta strandi29 – 313Combined sources
Helixi35 – 384Combined sources
Beta strandi47 – 6115Combined sources
Helixi62 – 643Combined sources
Beta strandi66 – 694Combined sources
Helixi74 – 807Combined sources
Helixi83 – 9210Combined sources
Helixi98 – 11013Combined sources
Helixi116 – 1227Combined sources
Helixi131 – 1399Combined sources
Helixi140 – 1445Combined sources
Helixi147 – 1493Combined sources
Beta strandi152 – 1543Combined sources
Helixi155 – 18127Combined sources
Beta strandi190 – 1923Combined sources
Helixi194 – 20310Combined sources
Beta strandi206 – 2083Combined sources
Helixi214 – 22512Combined sources
Helixi234 – 24411Combined sources
Helixi249 – 26113Combined sources
Turni262 – 2654Combined sources
Helixi268 – 27811Combined sources
Beta strandi281 – 2844Combined sources
Turni285 – 2884Combined sources
Helixi290 – 2923Combined sources
Helixi300 – 3023Combined sources
Helixi316 – 32914Combined sources
Helixi331 – 3333Combined sources
Turni335 – 3384Combined sources
Helixi339 – 34911Combined sources
Helixi351 – 3566Combined sources
Helixi362 – 37211Combined sources
Helixi379 – 40325Combined sources
Beta strandi410 – 4134Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABH7.

Family & Domainsi

Sequence similaritiesi

Belongs to the citrate synthase family.Curated

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021224.
InParanoidiP0ABH7.
KOiK01647.
OMAiNKEDGVR.
OrthoDBiEOG6P8TP4.
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-like.
IPR016141. Citrate_synthase-like_core.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111N → D AA sequence (PubMed:6380576)Curated
Sequence conflicti289 – 2891V → F in AAA23892. 1 PublicationCurated
Sequence conflicti289 – 2891V → F AA sequence (PubMed:6380576)Curated

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.
YP_489000.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73814; AAC73814; b0720.
BAA35384; BAA35384; BAA35384.
GeneIDi12930947.
945323.
KEGGiecj:Y75_p0700.
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.
YP_489000.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-36204N.
IntActiP0ABH7. 9 interactions.
MINTiMINT-1249502.
STRINGi511145.b0720.

Proteomic databases

PaxDbiP0ABH7.
PRIDEiP0ABH7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73814; AAC73814; b0720.
BAA35384; BAA35384; BAA35384.
GeneIDi12930947.
945323.
KEGGiecj:Y75_p0700.
eco:b0720.
PATRICi32116635. VBIEscCol129921_0750.

Organism-specific databases

EchoBASEiEB0397.
EcoGeneiEG10402. gltA.

Phylogenomic databases

eggNOGiCOG0372.
HOGENOMiHOG000021224.
InParanoidiP0ABH7.
KOiK01647.
OMAiNKEDGVR.
OrthoDBiEOG6P8TP4.
PhylomeDBiP0ABH7.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0ABH7.
PROiP0ABH7.

Gene expression databases

GenevestigatoriP0ABH7.

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-like.
IPR016141. Citrate_synthase-like_core.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequence of the gltA gene encoding citrate synthase in Escherichia coli."
    Ner S.S., Bhayana V., Bell A.W., Giles I.G., Duckworth H.W., Bloxham D.P.
    Biochemistry 22:5243-5249(1983)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Nucleotide sequence encoding the flavoprotein and hydrophobic subunits of the succinate dehydrogenase of Escherichia coli."
    Wood D., Darlison M.G., Wilde R.J., Guest J.R.
    Biochem. J. 222:519-534(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-127.
  6. "Amino acid sequence of Escherichia coli citrate synthase."
    Bhayana V., Duckworth H.W.
    Biochemistry 23:2900-2905(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-101; 110-217 AND 220-427.
  7. "Nucleotide sequence of the promoter region of the citrate synthase gene (gltA) of Escherichia coli."
    Hull E.P., Spencer M.E., Wood D., Guest J.R.
    FEBS Lett. 156:366-370(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98.
    Strain: K12.
  8. Guest J.R.
    Submitted (AUG-1984) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 92-94.
  9. "Transcript analysis of the citrate synthase and succinate dehydrogenase genes of Escherichia coli K12."
    Wilde R.J., Guest J.R.
    J. Gen. Microbiol. 132:3239-3251(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
    Strain: K12.
  10. "The synthesis and use of oligodeoxynucleotides in plasmid DNA sequencing."
    Ner S.S., Bloxham D.P., Handford P.A., Akhtar M.
    Int. J. Biochem. 18:257-262(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 360-388.
  11. "The role of cysteine 206 in allosteric inhibition of Escherichia coli citrate synthase. Studies by chemical modification, site-directed mutagenesis, and 19F NMR."
    Donald L.J., Crane B.R., Anderson D.H., Duckworth H.W.
    J. Biol. Chem. 266:20709-20713(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-207 AND GLU-208.
    Strain: ATCC 33694 / HB101.
  12. "icdB mutants of Escherichia coli."
    Helling R.B.
    J. Bacteriol. 177:2592-2593(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF ICDB AS GLTA.
  13. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  14. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.

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: January 7, 2015
This is version 84 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

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.