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Q6S9V7

- CISY_KATPE

UniProt

Q6S9V7 - CISY_KATPE

Protein

Citrate synthase, mitochondrial

Gene

cs

Organism
Katsuwonus pelamis (Skipjack tuna) (Bonito)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 46 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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 sitei350 – 3501PROSITE-ProRule annotation
    Active sitei405 – 4051PROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB
    2. cellular carbohydrate metabolic process Source: InterPro
    3. 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, mitochondrial (EC:2.3.3.1)
    Alternative name(s):
    Citrate (Si)-synthase
    Gene namesi
    Name:cs
    OrganismiKatsuwonus pelamis (Skipjack tuna) (Bonito)
    Taxonomic identifieri8226 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataPelagimorphariaScombriformesScombridaeKatsuwonus

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030MitochondrionBy similarityAdd
    BLAST
    Chaini31 – 469439Citrate synthase, mitochondrialPRO_0000253903Add
    BLAST

    Proteomic databases

    PRIDEiQ6S9V7.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ6S9V7.
    SMRiQ6S9V7. Positions 31-467.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    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.
    IPR010109. Citrate_synthase_euk.
    [Graphical view]
    PANTHERiPTHR11739. PTHR11739. 1 hit.
    PfamiPF00285. Citrate_synt. 1 hit.
    [Graphical view]
    PRINTSiPR00143. CITRTSNTHASE.
    SUPFAMiSSF48256. SSF48256. 1 hit.
    TIGRFAMsiTIGR01793. cit_synth_euk. 1 hit.
    PROSITEiPS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q6S9V7-1 [UniParc]FASTAAdd to Basket

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    MSFLSVSRLA PKLLNSKNAT YFLVAARNAS ASTTNLKDVL SDLIPKEQSR    50
    IKNFKQQYGK TNIGQITVDM VYGGMRGMKG LVYETSVLDP EEGIRFRGYS 100
    IPECQKLLPK APGGEEPLPE GLFWLLVTGQ VPTEEQVKWV SKEWAKRAAL 150
    PSHVVTMLDN FPTNLHPMSQ FSAAITALNS ESSFARAYSE GVHKTKYWEF 200
    VYEDSMDLIA KLPCIAAKIY RNLYREGSSI GAIDSNLDWS HNFTNMLGYS 250
    EAQFTELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL SFSAAMNGLA 300
    GPLHGLANQE VLVWLTALQK EMGGEVSDER MRDYIWNTLK SGRVVPGYGH 350
    AVLRKTDPRY TCQREFALKH LPNDPMFKLV AQLYKIVPNV LLEQGKAKNP 400
    WPNVDAHSGV LLQYYGMTEM NYYTVLFGVS RALGVLAQLV WSRALGFPLE 450
    RPKSMSTDGL MTLVGAKSG 469
    Length:469
    Mass (Da):52,207
    Last modified:July 5, 2004 - v1
    Checksum:i39C25C2F81DB2CF9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY461850 mRNA. Translation: AAR98860.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY461850 mRNA. Translation: AAR98860.1 .

    3D structure databases

    ProteinModelPortali Q6S9V7.
    SMRi Q6S9V7. Positions 31-467.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q6S9V7.

    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.
    IPR010109. Citrate_synthase_euk.
    [Graphical view ]
    PANTHERi PTHR11739. PTHR11739. 1 hit.
    Pfami PF00285. Citrate_synt. 1 hit.
    [Graphical view ]
    PRINTSi PR00143. CITRTSNTHASE.
    SUPFAMi SSF48256. SSF48256. 1 hit.
    TIGRFAMsi TIGR01793. cit_synth_euk. 1 hit.
    PROSITEi PS00480. CITRATE_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mitochondrial enzyme content in the muscles of high-performance fish: evolution and variation among fiber types."
      Dalziel A.C., Moore S.E., Moyes C.D.
      Am. J. Physiol. 288:R163-R172(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Red muscle.

    Entry informationi

    Entry nameiCISY_KATPE
    AccessioniPrimary (citable) accession number: Q6S9V7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 46 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.

    Documents

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

    External Data

    Dasty 3