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P51031

- CISY_BARBA

UniProt

P51031 - CISY_BARBA

Protein

Citrate synthase

Gene

gltA

Organism
Bartonella bacilliformis
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei248 – 2481PROSITE-ProRule annotation
    Active sitei306 – 3061PROSITE-ProRule annotation

    GO - Molecular functioni

    1. citrate (Si)-synthase activity Source: InterPro

    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

    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase (EC:2.3.3.16)
    Gene namesi
    Name:gltA
    OrganismiBartonella bacilliformis
    Taxonomic identifieri774 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›321›321Citrate synthasePRO_0000169931Add
    BLAST

    Proteomic databases

    PRIDEiP51031.

    Structurei

    3D structure databases

    ProteinModelPortaliP51031.
    SMRiP51031. Positions 1-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    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: Fragment.

    P51031-1 [UniParc]FASTAAdd to Basket

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    YIDGDEGILL YHGYSIDQLA ENGDFLETCY LLLYGELPNK QQKIDFDRCI    50
    MRHTMVHEQF ARFFHGFRRD SHPMAVMVAC LGAMSAFYHD SINITDPQQR 100
    MIASIRLISK VPTLAAMAYK YSIGQPFVYP RNDLNYATNF LHMCFSVPCE 150
    EHKISPVIAR AMDRIFTLHA DHEQNASTST VRLAGSSGAN PYACIAAGVA 200
    CLWGPAHGGA NEACLKMLQE IGSVKKIPEF IARAKDKNDP FRLMGFGHRV 250
    YKNYDPRAKI MQKTCHEVLQ ELNIQDDPLL DIAMELEHIA LNDEYFINKK 300
    LYPNVDFYSG ITLKALGFPT E 321
    Length:321
    Mass (Da):36,372
    Last modified:November 1, 1997 - v2
    Checksum:iD61068C82AB6B550
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Sequence conflicti229 – 2291E → Q in AAA74976. 1 PublicationCurated
    Sequence conflicti270 – 2701Q → K in AAA74976. 1 PublicationCurated
    Sequence conflicti277 – 2771D → N in AAA74976. 1 PublicationCurated
    Sequence conflicti280 – 2801L → F in AAA74976. 1 PublicationCurated
    Non-terminal residuei321 – 3211

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z70021 Genomic DNA. Translation: CAA93843.1.
    U28076 Genomic DNA. Translation: AAA74976.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z70021 Genomic DNA. Translation: CAA93843.1 .
    U28076 Genomic DNA. Translation: AAA74976.1 .

    3D structure databases

    ProteinModelPortali P51031.
    SMRi P51031. Positions 1-320.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P51031.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .

    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. "Comparison of partial citrate synthase gene (gltA) sequences for phylogenetic analysis of Bartonella species."
      Birtles R.J., Raoult D.
      Int. J. Syst. Bacteriol. 46:891-897(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-303.
      Strain: LA6.3.
    2. Jones D.C., Regnery R., Bowen M.
      Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 210-321.
      Strain: KC584 / ATCC 35686.

    Entry informationi

    Entry nameiCISY_BARBA
    AccessioniPrimary (citable) accession number: P51031
    Secondary accession number(s): Q59184
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 65 of the entry and version 2 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.

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3