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P51039

- CISY_RICAU

UniProt

P51039 - CISY_RICAU

Protein

Citrate synthase

Gene

gltA

Organism
Rickettsia australis
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 66 (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 sitei304 – 3041PROSITE-ProRule annotation
    Active sitei363 – 3631PROSITE-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
    OrganismiRickettsia australis
    Taxonomic identifieri787 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›411›411Citrate synthasePRO_0000169958Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP51039.
    SMRiP51039. Positions 5-411.
    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.

    P51039-1 [UniParc]FASTAAdd to Basket

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    DSEFAELKIR GKIFKLPILK ASIGEDVIDI SRVSAEADCF TYDPGFMSTA    50
    SCQSTITYID GDKGILRHRG YNIKDLAEKS DFLEVAYLLI YGELPTIEQY 100
    NNFTTQVAHH SLVNERLHYL FQAFCSSSHP MAIMLAAVGS LSAFYPDLLN 150
    FKEADYELTA IRMIAKIPTI AAMSYKYSIG QPFIYPDNSL DFTENFLHMM 200
    FATPCTKYKV NPIIKNALNK IFILHADHEQ NASTSTVRIA GSSGANAFAC 250
    ISTGIASLWG PAHGGANEAV INMLKEIGSS ENIPKFIAKA KDKNDPFRLM 300
    GFGHRVYKNY DPRAAVLKET CKAVLKELGQ LENNPLLQIA IELEAIALKD 350
    EYFIERKLYP NVDFYSGIIY KAMGIPSQMF TVLFAIARTV GWMAQWKEMH 400
    EDPEQKISRP R 411
    Length:411
    Mass (Da):46,112
    Last modified:November 1, 1997 - v2
    Checksum:i9D0571AFD3B6B27D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Sequence conflicti290 – 2901A → V in AAB49576. 1 PublicationCurated
    Sequence conflicti316 – 3161V → A in AAB49576. 1 PublicationCurated
    Sequence conflicti364 – 3652FY → SH in AAB49576. 1 PublicationCurated
    Sequence conflicti380 – 3801F → S in AAB49576. 1 PublicationCurated
    Non-terminal residuei411 – 4111

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59718 Genomic DNA. Translation: AAB02954.1.
    U33923 Genomic DNA. Translation: AAB49576.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59718 Genomic DNA. Translation: AAB02954.1 .
    U33923 Genomic DNA. Translation: AAB49576.1 .

    3D structure databases

    ProteinModelPortali P51039.
    SMRi P51039. Positions 5-411.
    ModBasei Search...
    MobiDBi Search...

    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. "Citrate synthase gene comparison, a new tool for phylogenetic analysis, and its application for the rickettsiae."
      Roux V., Rydkina E., Eremeeva M., Raoult D.
      Int. J. Syst. Bacteriol. 47:252-261(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Phillips.
    2. Higgins J.A., Radulovic S., Schriefer M.E.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-383.
      Strain: JC.

    Entry informationi

    Entry nameiCISY_RICAU
    AccessioniPrimary (citable) accession number: P51039
    Secondary accession number(s): Q59731
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 66 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