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Q0GNE0

- CISY_IGUIG

UniProt

Q0GNE0 - CISY_IGUIG

Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Iguana iguana (Common iguana)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 33 (01 Oct 2014)
      Sequence version 1 (03 Oct 2006)
      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
    OrganismiIguana iguana (Common iguana)
    Taxonomic identifieri8517 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiLepidosauriaSquamataBifurcataUnidentataEpisquamataToxicoferaIguaniaIguanidaeIguaninaeIguana

    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 – 3131MitochondrionBy similarityAdd
    BLAST
    Chaini32 – 469438Citrate synthase, mitochondrialPRO_0000253901Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ0GNE0.
    SMRiQ0GNE0. Positions 33-460.
    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.

    Q0GNE0-1 [UniParc]FASTAAdd to Basket

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    MTLLTASSRA AARLLGAKNS SCIIFAARHA STSTNLKDVL ANMIPKEQAR    50
    IKSFRQQYGS TVIGQITVDM LYGGMRGMKG LIYETSVLDP DEGIRFRGYS 100
    IPECQKLLPK APGGAEPLPE GLFWLLVTGE IPSQEQVNWV SREWAKRAAL 150
    PSHVVTMLDN FPTNLHPMSQ LSAAVTALNS ESTFARAYSE GISRTKYWEF 200
    IYEDSMDLIA KLPCIAAKIY RNLYREGSSI GAIDPALDWS HNFTNMLGYT 250
    DPQFIELMRL YLTIHSDHEG GNVSAHTSHL VGSALSDPYL AFAAAMNGLA 300
    GPLHGLANQE VLVWLTNLQK ELGEDVSDQK LRDFIWNTLN SGRVVPGYGH 350
    AVLRKTDPRY TCQREFALKH LPKDPLFKLV AQLYKIVPNV LLEQGKAKNP 400
    WPNVDAHSGV LLQYYGMKEM NYYTVLFGVS RALGVLSQLI WSRALGFPLE 450
    RPKSMSTDGL MVLVGAKSG 469
    Length:469
    Mass (Da):51,957
    Last modified:October 3, 2006 - v1
    Checksum:i40C89727DCADD889
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ829808 mRNA. Translation: ABI21882.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ829808 mRNA. Translation: ABI21882.1 .

    3D structure databases

    ProteinModelPortali Q0GNE0.
    SMRi Q0GNE0. Positions 33-460.
    ModBasei Search...
    MobiDBi Search...

    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. "Temperature adaptation in muscle-type lactate dehydrogenase and citrate synthase of Amblyrhynchus cristatus, the Galapagos marine iguana."
      Fields P.A., Strothers C.M.
      Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiCISY_IGUIG
    AccessioniPrimary (citable) accession number: Q0GNE0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 33 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