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Q1RHL6

- FUMC_RICBR

UniProt

Q1RHL6 - FUMC_RICBR

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Rickettsia bellii (strain RML369-C)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 59 (01 Oct 2014)
      Sequence version 1 (16 May 2006)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible addition of water to fumarate to give L-malate.By similarity

    Catalytic activityi

    (S)-malate = fumarate + H2O.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei188 – 1881Proton donor/acceptorBy similarity
    Active sitei318 – 3181By similarity
    Binding sitei319 – 3191SubstrateUniRule annotation
    Sitei331 – 3311Important for catalytic activityBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. fumarate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    BioCyciRBEL336407:GJCY-1099-MONOMER.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase class IIUniRule annotation (EC:4.2.1.2UniRule annotation)
    Short name:
    Fumarase CUniRule annotation
    Gene namesi
    Name:fumCUniRule annotation
    Ordered Locus Names:RBE_1067
    OrganismiRickettsia bellii (strain RML369-C)
    Taxonomic identifieri336407 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiabelli group
    ProteomesiUP000001951: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 463463Fumarate hydratase class IIPRO_0000277938Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi336407.RBE_1067.

    Structurei

    3D structure databases

    ProteinModelPortaliQ1RHL6.
    SMRiQ1RHL6. Positions 3-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1003Substrate bindingUniRule annotation
    Regioni129 – 1324B siteUniRule annotation
    Regioni139 – 1413Substrate bindingUniRule annotation
    Regioni187 – 1882Substrate bindingUniRule annotation
    Regioni324 – 3263Substrate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiMESFNIH.
    OrthoDBiEOG6V1M4M.

    Family and domain databases

    Gene3Di1.10.275.10. 1 hit.
    HAMAPiMF_00743. FumaraseC.
    InterProiIPR005677. Fum_hydII.
    IPR024083. Fumarase/histidase_N.
    IPR018951. Fumarase_C_C.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SUPFAMiSSF48557. SSF48557. 1 hit.
    TIGRFAMsiTIGR00979. fumC_II. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q1RHL6-1 [UniParc]FASTAAdd to Basket

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    MTNYRTESDS FGEIQIEDKF YWGAQTQRSL ENFKIGKQRM PEILIRSLAI    50
    LKKCAAKVNL EFGDLEPKIA ESIDKATSRI LNAEFSDNFP LVVWQTGSGT 100
    QTNMNMNEVI ASIANEELTG MKGGKSPVHP NDHVNKGQSS NDSFPTAMHI 150
    ATVLATREKL IPALNNLLTA LQNKSKDWDS IIKIGRTHLQ DATPLTLKQE 200
    FSGYITQIEY ALERIEDALK KVYLLAQGGT AVGTGINSRK GFDIKFAEEV 250
    AEFTKQPFKT APNKFESLAA HDALVEFSGT LNTIAVSLMK IANDIRLLGS 300
    GPRCGLGELH LPENEPGSSI MPGKVNPTQV EALTMVCTQV MGNHVTVTIA 350
    GSNGHLELNV FKPVIIYNIL QSIELLSDAA NSFVTHCVDG IEPNITHIND 400
    LRDKSLMLVT ALNPHIGYDN AAKIAKEAHK HGITLKEAAK KLNLLSEEEF 450
    NKIVVPEKMV RQS 463
    Length:463
    Mass (Da):50,903
    Last modified:May 16, 2006 - v1
    Checksum:i13988722F6B3A0BC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000087 Genomic DNA. Translation: ABE05148.1.
    RefSeqiYP_538237.1. NC_007940.1.

    Genome annotation databases

    EnsemblBacteriaiABE05148; ABE05148; RBE_1067.
    GeneIDi3995904.
    KEGGirbe:RBE_1067.
    PATRICi17883701. VBIRicBel102610_1204.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000087 Genomic DNA. Translation: ABE05148.1 .
    RefSeqi YP_538237.1. NC_007940.1.

    3D structure databases

    ProteinModelPortali Q1RHL6.
    SMRi Q1RHL6. Positions 3-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 336407.RBE_1067.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABE05148 ; ABE05148 ; RBE_1067 .
    GeneIDi 3995904.
    KEGGi rbe:RBE_1067.
    PATRICi 17883701. VBIRicBel102610_1204.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi MESFNIH.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci RBEL336407:GJCY-1099-MONOMER.

    Family and domain databases

    Gene3Di 1.10.275.10. 1 hit.
    HAMAPi MF_00743. FumaraseC.
    InterProi IPR005677. Fum_hydII.
    IPR024083. Fumarase/histidase_N.
    IPR018951. Fumarase_C_C.
    IPR020557. Fumarate_lyase_CS.
    IPR000362. Fumarate_lyase_fam.
    IPR022761. Fumarate_lyase_N.
    IPR008948. L-Aspartase-like.
    [Graphical view ]
    PANTHERi PTHR11444. PTHR11444. 1 hit.
    Pfami PF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00149. FUMRATELYASE.
    SUPFAMi SSF48557. SSF48557. 1 hit.
    TIGRFAMsi TIGR00979. fumC_II. 1 hit.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of Rickettsia bellii illuminates the role of amoebae in gene exchanges between intracellular pathogens."
      Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., Fournier P.-E., Claverie J.-M., Raoult D.
      PLoS Genet. 2:733-744(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: RML369-C.

    Entry informationi

    Entry nameiFUMC_RICBR
    AccessioniPrimary (citable) accession number: Q1RHL6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: May 16, 2006
    Last modified: October 1, 2014
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity.By similarity

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Rickettsia bellii strain RML369-C
      Rickettsia bellii (strain RML369-C): entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3