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P51038

- CISY2_RHITR

UniProt

P51038 - CISY2_RHITR

Protein

Citrate synthase, plasmid

Gene

pcsA

Organism
Rhizobium tropici
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    The exact function of the plasmid-encoded citrate synthase is not clear, it could help nodulation by allowing the bacteria to use citrate as a chelator of iron and calcium.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei306 – 3061PROSITE-ProRule annotation
    Active sitei364 – 3641PROSITE-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, plasmid (EC:2.3.3.16)
    Gene namesi
    Name:pcsA
    Encoded oniPlasmid sym0 Publication
    OrganismiRhizobium tropici
    Taxonomic identifieri398 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: InterPro

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 429429Citrate synthase, plasmidPRO_0000169955Add
    BLAST

    Proteomic databases

    PRIDEiP51038.
    ProMEXiP51038.

    Structurei

    3D structure databases

    ProteinModelPortaliP51038.
    SMRiP51038. Positions 4-429.
    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: Complete.

    P51038-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNNNACVLV DGHSAELKLR SSTIGPNVLG IGSLYEQTKM FTYDPGFTST    50
    ASCESSITFI DGDEGVLLHR GYPIEQLAEH GDFLEVCYLL LYGELPTAAQ 100
    KKDFDYRVVH HTMVHEQMSR FFTGFRRDAH PMAVMCGCVG ALSAFYHDST 150
    DITDPHQRMV ASLRMIAKMP TLAAMAYKYH IGQPFVYPKN DLDYASNFLR 200
    MCFAVPCEEY VVNPVLARAM DRIFILHADH EQNASTSTVR LAGSSGANPF 250
    ACIAAGIACL WGPAHGGANE RALNMLTEIG TVDRIPEYIA RAKDKNDPFR 300
    LMGFGHRVYK NYDPRAKIMQ KTAHEVLGEL GIKDDPLLDI AIELERIALT 350
    DDYFIEKKLY PNVDFYSGIT LKALGFPTTM FTVLFALART VGWIAQWNEM 400
    IEDPDQRIGR PRQLYTGAPL REYVPLSKR 429
    Length:429
    Mass (Da):48,105
    Last modified:October 1, 1996 - v1
    Checksum:iC2E4560E4FE03485
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z34516 Genomic DNA. Translation: CAA84274.1.
    PIRiS41527.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z34516 Genomic DNA. Translation: CAA84274.1 .
    PIRi S41527.

    3D structure databases

    ProteinModelPortali P51038.
    SMRi P51038. Positions 4-429.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P51038.
    ProMEXi P51038.

    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. "Nodulating ability of Rhizobium tropici is conditioned by a plasmid-encoded citrate synthase."
      Pardo M.A., Lagunez J., Miranda J., Martinez E.
      Mol. Microbiol. 11:315-321(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CFN 299.

    Entry informationi

    Entry nameiCISY2_RHITR
    AccessioniPrimary (citable) accession number: P51038
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Plasmid

    Documents

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

    External Data

    Dasty 3