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P14165

- CISY_PSEAE

UniProt

P14165 - CISY_PSEAE

Protein

Citrate synthase

Gene

gltA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (08 Dec 2000)
      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. citrate synthase activity Source: PseudoCAP

    GO - Biological processi

    1. cellular carbohydrate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: PseudoCAP

    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
    Ordered Locus Names:PA1580
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA1580.

    Subcellular locationi

    GO - Cellular componenti

    1. tricarboxylic acid cycle enzyme complex Source: PseudoCAP

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 428428Citrate synthasePRO_0000169952Add
    BLAST

    Proteomic databases

    PRIDEiP14165.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    STRINGi208964.PA1580.

    Structurei

    3D structure databases

    ProteinModelPortaliP14165.
    SMRiP14165. Positions 3-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000021224.
    KOiK01647.
    OMAiKETCDEV.
    OrthoDBiEOG6P8TP4.
    PhylomeDBiP14165.

    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.

    P14165-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADKKAQLII EGSAPVELPV LSGTMGPDVV DVRGLTATGH FTFDPGFMST    50
    ASCESKITYI DGDKGVLLHR GYPIEQLAEK SDYLETCYLL LNGELPTAAQ 100
    KEQFVGTIKN HTMVHEQLKT FFNGFRRDAH PMAVMCGVIG ALSAFYHDSL 150
    DINNPKHREV SAHRLIAKMP TIAAMVYKYS KGEPMMYPRN DLNYAENFLH 200
    MMFNTPCETK PISPVLAKAM DRIFILHADH EQNASTSTVR LAGSSGANPF 250
    ACIASGIAAL WGPAHGGANE AVLRMLDEIG DVSNIDKFVE KAKDKNDPFK 300
    LMGFGHRVYK NFDPRAKVMK QTCDEVLQEL GINDPQLELA MKLEEIARHD 350
    PYFVERNLYP NVDFYSGIIL KAIGIPTSMF TVIFALARTV GWISHWQEML 400
    SGPYKIGRPR QLYTGHTQRD FTALKDRG 428
    Length:428
    Mass (Da):47,695
    Last modified:December 8, 2000 - v2
    Checksum:i3E1875ED70266C37
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti153 – 1531N → T in AAA25769. (PubMed:2507528)Curated
    Sequence conflicti159 – 1591E → Q in AAA25769. (PubMed:2507528)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29728 Genomic DNA. Translation: AAA25769.1.
    AE004091 Genomic DNA. Translation: AAG04969.1.
    PIRiA33596. YKPSCA.
    B83448.
    RefSeqiNP_250271.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG04969; AAG04969; PA1580.
    GeneIDi882117.
    KEGGipae:PA1580.
    PATRICi19837506. VBIPseAer58763_1639.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29728 Genomic DNA. Translation: AAA25769.1 .
    AE004091 Genomic DNA. Translation: AAG04969.1 .
    PIRi A33596. YKPSCA.
    B83448.
    RefSeqi NP_250271.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali P14165.
    SMRi P14165. Positions 3-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA1580.

    Proteomic databases

    PRIDEi P14165.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG04969 ; AAG04969 ; PA1580 .
    GeneIDi 882117.
    KEGGi pae:PA1580.
    PATRICi 19837506. VBIPseAer58763_1639.

    Organism-specific databases

    PseudoCAPi PA1580.

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000021224.
    KOi K01647.
    OMAi KETCDEV.
    OrthoDBi EOG6P8TP4.
    PhylomeDBi P14165.

    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. "Cloning, sequencing, and expression of the gene for NADH-sensitive citrate synthase of Pseudomonas aeruginosa."
      Donald L.J., Molgat G.F., Duckworth H.W.
      J. Bacteriol. 171:5542-5550(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiCISY_PSEAE
    AccessioniPrimary (citable) accession number: P14165
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: December 8, 2000
    Last modified: October 1, 2014
    This is version 107 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.

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3