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P0ABH7

- CISY_ECOLI

UniProt

P0ABH7 - CISY_ECOLI

Protein

Citrate synthase

Gene

gltA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (25 Oct 2005)
      Previous versions | rss
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    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
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    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

    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 – 64
    Beta strandi8 – 1811
    Beta strandi24 – 263
    Beta strandi29 – 313
    Helixi35 – 384
    Beta strandi47 – 6115
    Helixi62 – 643
    Beta strandi66 – 694
    Helixi74 – 807
    Helixi83 – 9210
    Helixi98 – 11013
    Helixi116 – 1227
    Helixi131 – 1399
    Helixi140 – 1445
    Helixi147 – 1493
    Beta strandi152 – 1543
    Helixi155 – 18127
    Beta strandi190 – 1923
    Helixi194 – 20310
    Beta strandi206 – 2083
    Helixi214 – 22512
    Helixi234 – 24411
    Helixi249 – 26113
    Turni262 – 2654
    Helixi268 – 27811
    Beta strandi281 – 2844
    Turni285 – 2884
    Helixi290 – 2923
    Helixi300 – 3023
    Helixi316 – 32914
    Helixi331 – 3333
    Turni335 – 3384
    Helixi339 – 34911
    Helixi351 – 3566
    Helixi362 – 37211
    Helixi379 – 40325
    Beta strandi410 – 4134

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK01647.
    OMAiKETCDEV.
    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

    MADTKAKLTL NGDTAVELDV LKGTLGQDVI DIRTLGSKGV FTFDPGFTST    50
    ASCESKITFI DGDEGILLHR GFPIDQLATD SNYLEVCYIL LNGEKPTQEQ 100
    YDEFKTTVTR HTMIHEQITR LFHAFRRDSH PMAVMCGITG ALAAFYHDSL 150
    DVNNPRHREI AAFRLLSKMP TMAAMCYKYS IGQPFVYPRN DLSYAGNFLN 200
    MMFSTPCEPY EVNPILERAM DRILILHADH EQNASTSTVR TAGSSGANPF 250
    ACIAAGIASL WGPAHGGANE AALKMLEEIS SVKHIPEFVR RAKDKNDSFR 300
    LMGFGHRVYK NYDPRATVMR ETCHEVLKEL GTKDDLLEVA MELENIALND 350
    PYFIEKKLYP NVDFYSGIIL KAMGIPSSMF TVIFAMARTV GWIAHWSEMH 400
    SDGMKIARPR QLYTGYEKRD FKSDIKR 427
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi G64807. YKEC.
    RefSeqi NP_415248.1. NC_000913.3.
    YP_489000.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NXE X-ray 2.30 A/B 1-427 [» ]
    1NXG X-ray 2.50 A/B 1-427 [» ]
    1OWB X-ray 2.20 A/B 1-427 [» ]
    1OWC X-ray 2.20 A/B 1-427 [» ]
    4G6B X-ray 2.20 A/B 2-427 [» ]
    4JAD X-ray 1.90 A/B 2-427 [» ]
    4JAE X-ray 2.70 A/B 2-427 [» ]
    4JAF X-ray 2.30 A/B 2-427 [» ]
    4JAG X-ray 2.10 A/B 2-427 [» ]
    ProteinModelPortali P0ABH7.
    SMRi P0ABH7. Positions 2-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-36204N.
    IntActi P0ABH7. 9 interactions.
    MINTi MINT-1249502.
    STRINGi 511145.b0720.

    Proteomic databases

    PaxDbi P0ABH7.
    PRIDEi P0ABH7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73814 ; AAC73814 ; b0720 .
    BAA35384 ; BAA35384 ; BAA35384 .
    GeneIDi 12930947.
    945323.
    KEGGi ecj:Y75_p0700.
    eco:b0720.
    PATRICi 32116635. VBIEscCol129921_0750.

    Organism-specific databases

    EchoBASEi EB0397.
    EcoGenei EG10402. gltA.

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000021224.
    KOi K01647.
    OMAi KETCDEV.
    OrthoDBi EOG6P8TP4.
    PhylomeDBi P0ABH7.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    BioCyci EcoCyc:CITSYN-MONOMER.
    ECOL316407:JW0710-MONOMER.
    MetaCyc:CITSYN-MONOMER.
    SABIO-RK P0ABH7.

    Miscellaneous databases

    EvolutionaryTracei P0ABH7.
    PROi P0ABH7.

    Gene expression databases

    Genevestigatori P0ABH7.

    Family and domain databases

    Gene3Di 1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProi IPR016142. 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 ]
    PANTHERi PTHR11739. PTHR11739. 1 hit.
    Pfami PF00285. Citrate_synt. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001369. Citrate_synth. 1 hit.
    PRINTSi PR00143. CITRTSNTHASE.
    SUPFAMi SSF48256. SSF48256. 1 hit.
    TIGRFAMsi TIGR01798. cit_synth_I. 1 hit.
    PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 81 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