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A4H9H8

- CISY_LEIBR

UniProt

A4H9H8 - CISY_LEIBR

Protein

Probable citrate synthase, mitochondrial

Gene

LbrM18_V2.0760

Organism
Leishmania braziliensis
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (01 May 2007)
      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 sitei297 – 2971PROSITE-ProRule annotation
    Active sitei351 – 3511PROSITE-ProRule annotation
    Active sitei406 – 4061PROSITE-ProRule annotation

    GO - Molecular functioni

    1. transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer 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

    UniPathwayiUPA00223; UER00717.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable citrate synthase, mitochondrial (EC:2.3.3.16)
    Gene namesi
    ORF Names:LbrM18_V2.0760, LbrM_18_0760
    OrganismiLeishmania braziliensis
    Taxonomic identifieri5660 [NCBI]
    Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmaniaLeishmania braziliensis species complex
    ProteomesiUP000007258: Chromosome 18

    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? – 470Probable citrate synthase, mitochondrialPRO_0000291604
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliA4H9H8.
    SMRiA4H9H8. Positions 23-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the citrate synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    KOiK01647.
    OMAiELIYEDC.

    Family and domain databases

    Gene3Di1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProiIPR016142. Citrate_synth-like_lrg_a-sub.
    IPR016143. Citrate_synth-like_sm_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: Complete.

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

    A4H9H8-1 [UniParc]FASTAAdd to Basket

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    MRAARCSIIR GAAGLRMASS VMSEMKEQML KRSKVEKQTI SELRKKHGDV    50
    KLSDASIDAA YCGMRGITGL VYEPSLLDPV EGIRFRNRTI PECQEVLPKA 100
    PNGCETLPEA MFWLLMTGEV PTAEQARALN AELHRRADPV AIAAAQKAIA 150
    ALPASTHPMT AFSVGVLALQ TYSKFAAAYA TGKSNKTTYW EYALEDSLDM 200
    LARTPAVAAM IYNRVTKGRA EVAASSNSEL DWAANFSNML GFKDNEFWEC 250
    MRLYLSIHVD HEGGNVSAHT TTLVASALSD PYLAFSAGLN GLAGPLHGLA 300
    NQEVLKYLLS MQDRVKADGV NVCDEAALEV ALTKYTWELL NSGQVVPGYG 350
    HAVLRKVDPR YTCLRNFCLR HHFEDDLFKL INIIYKIMPG ILTEHGKTKN 400
    PYPNVDAHSG VLLQHYGLTE QDYYTVLFGL SRQMGVMAGV VWDRLQGRPL 450
    ERPKSITTEM LAKKYLCTPR 470
    Length:470
    Mass (Da):51,957
    Last modified:May 1, 2007 - v1
    Checksum:iD1EFE121FC034466
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FR798992 Genomic DNA. Translation: CAM38050.1.
    RefSeqiXP_001564000.1. XM_001563950.1.

    Genome annotation databases

    GeneIDi5414535.
    KEGGilbz:LBRM_18_0760.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    FR798992 Genomic DNA. Translation: CAM38050.1 .
    RefSeqi XP_001564000.1. XM_001563950.1.

    3D structure databases

    ProteinModelPortali A4H9H8.
    SMRi A4H9H8. Positions 23-463.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 5414535.
    KEGGi lbz:LBRM_18_0760.

    Phylogenomic databases

    KOi K01647.
    OMAi ELIYEDC.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER00717 .

    Family and domain databases

    Gene3Di 1.10.230.10. 1 hit.
    1.10.580.10. 1 hit.
    InterProi IPR016142. Citrate_synth-like_lrg_a-sub.
    IPR016143. Citrate_synth-like_sm_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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MHOM/BR/75/M2904.

    Entry informationi

    Entry nameiCISY_LEIBR
    AccessioniPrimary (citable) accession number: A4H9H8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 48 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3