Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0ABH7 (CISY_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Citrate synthase

EC=2.3.3.16
Gene names
Name:gltA
Synonyms:gluT, icdB
Ordered Locus Names:b0720, JW0710
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.

Enzyme regulation

Allosterically inhibited by NADH.

Pathway

Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2.

Subunit structure

Homohexamer.

Miscellaneous

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

Sequence similarities

Belongs to the citrate synthase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself5EBI-547808,EBI-547808
yegSP764072EBI-547808,EBI-1127478

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 427427Citrate synthase
PRO_0000169943

Sites

Active site3061 By similarity
Active site3631 By similarity

Amino acid modifications

Modified residue2831N6-acetyllysine Ref.14

Experimental info

Mutagenesis2071C → S: Weakened NADH binding and inhibition. Ref.11
Mutagenesis2081E → A: Weakened NADH binding and inhibition. Ref.11
Sequence conflict111N → D AA sequence Ref.6
Sequence conflict2891V → F in AAA23892. Ref.1
Sequence conflict2891V → F AA sequence Ref.6

Secondary structure

..................................................................... 427
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABH7 [UniParc].

Last modified October 25, 2005. Version 1.
Checksum: F30A9DBF1FC590D5

FASTA42748,015
        10         20         30         40         50         60 
MADTKAKLTL NGDTAVELDV LKGTLGQDVI DIRTLGSKGV FTFDPGFTST ASCESKITFI 

        70         80         90        100        110        120 
DGDEGILLHR GFPIDQLATD SNYLEVCYIL LNGEKPTQEQ YDEFKTTVTR HTMIHEQITR 

       130        140        150        160        170        180 
LFHAFRRDSH PMAVMCGITG ALAAFYHDSL DVNNPRHREI AAFRLLSKMP TMAAMCYKYS 

       190        200        210        220        230        240 
IGQPFVYPRN DLSYAGNFLN MMFSTPCEPY EVNPILERAM DRILILHADH EQNASTSTVR 

       250        260        270        280        290        300 
TAGSSGANPF ACIAAGIASL WGPAHGGANE AALKMLEEIS SVKHIPEFVR RAKDKNDSFR 

       310        320        330        340        350        360 
LMGFGHRVYK NYDPRATVMR ETCHEVLKEL GTKDDLLEVA MELENIALND PYFIEKKLYP 

       370        380        390        400        410        420 
NVDFYSGIIL KAMGIPSSMF TVIFAMARTV GWIAHWSEMH SDGMKIARPR QLYTGYEKRD 


FKSDIKR 

« Hide

References

« Hide 'large scale' references
[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]"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map."
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. expand/collapse author list , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRYKEC. G64807.
RefSeqNP_415248.1. NC_000913.3.
YP_489000.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP0ABH7.
SMRP0ABH7. Positions 2-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36204N.
IntActP0ABH7. 9 interactions.
MINTMINT-1249502.
STRING511145.b0720.

Proteomic databases

PaxDbP0ABH7.
PRIDEP0ABH7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73814; AAC73814; b0720.
BAA35384; BAA35384; BAA35384.
GeneID12930947.
945323.
KEGGecj:Y75_p0700.
eco:b0720.
PATRIC32116635. VBIEscCol129921_0750.

Organism-specific databases

EchoBASEEB0397.
EcoGeneEG10402. gltA.

Phylogenomic databases

eggNOGCOG0372.
HOGENOMHOG000021224.
KOK01647.
OMAKETCDEV.
OrthoDBEOG6P8TP4.
PhylomeDBP0ABH7.

Enzyme and pathway databases

BioCycEcoCyc:CITSYN-MONOMER.
ECOL316407:JW0710-MONOMER.
MetaCyc:CITSYN-MONOMER.
SABIO-RKP0ABH7.
UniPathwayUPA00223; UER00717.

Gene expression databases

GenevestigatorP0ABH7.

Family and domain databases

Gene3D1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
InterProIPR016142. 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-II.
[Graphical view]
PANTHERPTHR11739. PTHR11739. 1 hit.
PfamPF00285. Citrate_synt. 1 hit.
[Graphical view]
PIRSFPIRSF001369. Citrate_synth. 1 hit.
PRINTSPR00143. CITRTSNTHASE.
SUPFAMSSF48256. SSF48256. 1 hit.
TIGRFAMsTIGR01798. cit_synth_I. 1 hit.
PROSITEPS00480. CITRATE_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABH7.
PROP0ABH7.

Entry information

Entry nameCISY_ECOLI
AccessionPrimary (citable) accession number: P0ABH7
Secondary accession number(s): O32552, P00891, P78257
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 25, 2005
Last modified: June 11, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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