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P49298

- CISY_CITMA

UniProt

P49298 - CISY_CITMA

Protein

Citrate synthase, mitochondrial

Gene

CIT

Organism
Citrus maxima (Pomelo) (Citrus grandis)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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 sitei307 – 3071PROSITE-ProRule annotation
    Active sitei353 – 3531PROSITE-ProRule annotation
    Active sitei408 – 4081PROSITE-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

    BRENDAi2.3.3.1. 2323.
    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase, mitochondrial (EC:2.3.3.16)
    Gene namesi
    Name:CIT
    OrganismiCitrus maxima (Pomelo) (Citrus grandis)
    Taxonomic identifieri37334 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsSapindalesRutaceaeCitrus

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1818MitochondrionSequence AnalysisAdd
    BLAST
    Chaini19 – 471453Citrate synthase, mitochondrialPRO_0000005486Add
    BLAST

    Proteomic databases

    PRIDEiP49298.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP49298.
    SMRiP49298. Positions 35-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    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.

    P49298-1 [UniParc]FASTAAdd to Basket

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    MASLRSATAL SRLRSRAGQQ SNLSNSVRWL QMQSSADLDL HSQLKEMIPE    50
    QQERLKKVKS DLGKAQLGNI TIDVVIGGMR GMTGLLWETS LLDPDEGIRF 100
    RGLSIPECQK LLPAAKPDGE PLPEGLLWLL LTGKVPSKEQ VDGLSKELRD 150
    RATVPDYVYK AIDALPVSAH PMTQFASGVM ALQVQSEFQE AYEKGIHKSK 200
    SWEPTSEDSL NLIARVPVVA AYVYQRIYKD GKIIPKDDSL DYGGNFSHML 250
    GFDDPKMLEL MRLYVTIHSD HEGGNVSAHT GHLVASALSD PYLSFLAALN 300
    GLAGPLHGLA NQEVLLWIKS VVDECGENVT TEQLKDYVWK TLNSGKVVPG 350
    FGHGVLRKTD PRYTCQREFA LKHLPDDPLF QLVSKLYEVV PPILTKLGKV 400
    KNPWPNVDAH SGVLLNHFGL AEARYYTVLF GVSRSLGICS QLIWDRALGL 450
    PLERPKSVTL DWIEKNCKKA A 471
    Length:471
    Mass (Da):52,183
    Last modified:February 1, 1996 - v1
    Checksum:i8EE1E23F7E154806
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19481 mRNA. Translation: AAA82743.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19481 mRNA. Translation: AAA82743.1 .

    3D structure databases

    ProteinModelPortali P49298.
    SMRi P49298. Positions 35-465.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P49298.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    BRENDAi 2.3.3.1. 2323.

    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. Canel C.
      Thesis (1994), University of California Riverside, United States
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Siamese Sweet 2240.

    Entry informationi

    Entry nameiCISY_CITMA
    AccessioniPrimary (citable) accession number: P49298
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant 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