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O80433

- CISY_DAUCA

UniProt

O80433 - CISY_DAUCA

Protein

Citrate synthase, mitochondrial

Gene

CS

Organism
Daucus carota (Wild carrot)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      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 sitei308 – 3081PROSITE-ProRule annotation
    Active sitei354 – 3541PROSITE-ProRule annotation
    Active sitei409 – 4091PROSITE-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

    BioCyciMetaCyc:MONOMER-15824.
    BRENDAi2.3.3.1. 1841.
    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Citrate synthase, mitochondrial (EC:2.3.3.16)
    Gene namesi
    Name:CS
    OrganismiDaucus carota (Wild carrot)
    Taxonomic identifieri4039 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsApialesApiaceaeApioideaeScandiceaeDaucinaeDaucus

    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
    Chaini? – 472Citrate synthase, mitochondrialPRO_0000005487
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    PRIDEiO80433.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO80433.
    SMRiO80433. Positions 36-464.
    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.

    O80433-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVFFRSVSLL NKLRSRAVQQ SNLSNTVRWF QVQTSASDLD LRSQLKELIP    50
    EQQERIKKLK AEHGKVQLGN ITVDMVLGGM RGMTGLLWET SLLDPEEGIR 100
    FRGLSIPECQ KLLPGAKPGG EPLPEGLLWL LLTGKVPTKE QVDALSAELR 150
    SRAAVPEHVY KTIDALPVTA HPMTQFATGV MALQVQSEFQ KAYEKGIHKT 200
    KYWEPTYEDS ITLIAQLPVV AAYIYRRMYK NGQSISTDDS LDYGANFAHM 250
    LGYDSPSMQE LMRLYVTIHT DHEGGNVSAH TGHLVASALS DPYLSFAAAL 300
    NGLAGPLHGL ANQEVLLWIK SVVSECGENV TKEQLKDYIW KTLNSGKVVP 350
    GYGHGVLRNT DPRYICQREF ALKHLPDDPL FQLVSNLFEV VPPILTELGK 400
    VKNPWPNVDA HSGVLLNHYG LTEARYYTVL FGVSRAIGIC SQLVWDRALG 450
    LPLERPKSVT MEWLENHCKK SS 472
    Length:472
    Mass (Da):52,657
    Last modified:November 1, 1998 - v1
    Checksum:iA6C8CFCA17142120
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017159 mRNA. Translation: BAA32557.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017159 mRNA. Translation: BAA32557.1 .

    3D structure databases

    ProteinModelPortali O80433.
    SMRi O80433. Positions 36-464.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi O80433.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .
    BioCyci MetaCyc:MONOMER-15824.
    BRENDAi 2.3.3.1. 1841.

    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. "cDNA encoding carrot mitochondrial citrate synthase."
      Takita E., Koyama H., Shirano Y., Shibata D., Hara T.
      Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. MS Yonsun.

    Entry informationi

    Entry nameiCISY_DAUCA
    AccessioniPrimary (citable) accession number: O80433
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 76 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