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Q0QEL7

- CISY_MESAU

UniProt

Q0QEL7 - CISY_MESAU

Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 40 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Acetyl-CoA + H2O + oxaloacetate = citrate + CoA.By similarityPROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei74 – 741By similarityPROSITE-ProRule annotation
    Active sitei120 – 1201By similarityPROSITE-ProRule annotation
    Active sitei175 – 1751By similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. citrate (Si)-synthase activity Source: UniProtKB-EC

    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, mitochondrialBy similarity (EC:2.3.3.1)
    Alternative name(s):
    Citrate (Si)-synthase
    Gene namesi
    Name:CSImported
    OrganismiMesocricetus auratus (Golden hamster)
    Taxonomic identifieri10036 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›213›213Citrate synthase, mitochondrialPRO_0000394310Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei94 – 941N6-acetyllysine; alternateBy similarity
    Modified residuei94 – 941N6-succinyllysine; alternateBy similarity
    Modified residuei100 – 1001N6-acetyllysine; alternateBy similarity
    Modified residuei100 – 1001N6-succinyllysine; alternateBy similarity
    Modified residuei148 – 1481N6-acetyllysine; alternateBy similarity
    Modified residuei148 – 1481N6-succinyllysine; alternateBy similarity
    Modified residuei155 – 1551N6-acetyllysineBy similarity
    Modified residuei166 – 1661N6-acetyllysine; alternateBy similarity
    Modified residuei166 – 1661N6-succinyllysine; alternateBy similarity
    Modified residuei168 – 1681N6,N6,N6-trimethyllysineBy similarity

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    PRIDEiQ0QEL7.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Sequence Analysis

    Phylogenomic databases

    HOVERGENiHBG005336.

    Family and domain databases

    Gene3Di1.10.580.10. 1 hit.
    InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    [Graphical view]
    PANTHERiPTHR11739. PTHR11739. 1 hit.
    PfamiPF00285. Citrate_synt. 1 hit.
    [Graphical view]
    PRINTSiPR00143. CITRTSNTHASE.
    SUPFAMiSSF48256. SSF48256. 1 hit.
    PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    Q0QEL7-1 [UniParc]FASTAAdd to Basket

    « Hide

    GAIDSKLDWS HNFTNMLGYT EPQFTELMRL YLTIHSDHEG GNVSAHTSHL    50
    VGSALSDPYL SFAAAMNGLA GPLHGLANQE VLVWLTQLQK EVGKDVSDEK 100
    LRDYIWNTLN SGRVVPGYGH AVLRKTDPRY SCQREFALKH LPNDPLFKLV 150
    AQLYKIVPNI LLEQGKAKNP WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS 200
    RALGVLAQLI WSR 213
    Length:213
    Mass (Da):23,884
    Last modified:September 5, 2006 - v1
    Checksum:iF423CBF73DF89D63
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11Imported
    Non-terminal residuei213 – 2131Imported

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ403127 mRNA. Translation: ABD77260.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ403127 mRNA. Translation: ABD77260.1 .

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q0QEL7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG005336.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .

    Family and domain databases

    Gene3Di 1.10.580.10. 1 hit.
    InterProi IPR016142. Citrate_synth-like_lrg_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR019810. Citrate_synthase_AS.
    [Graphical view ]
    PANTHERi PTHR11739. PTHR11739. 1 hit.
    Pfami PF00285. Citrate_synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00143. CITRTSNTHASE.
    SUPFAMi SSF48256. SSF48256. 1 hit.
    PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
      Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
      Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: LiverImported.
    2. "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
      Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
      Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCISY_MESAU
    AccessioniPrimary (citable) accession number: Q0QEL7
    Secondary accession number(s): P86224
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 18, 2010
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 40 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Citrate synthase is found in nearly all cells capable of oxidative metabolism.Curated

    Documents

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

    External Data

    Dasty 3