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B2HT54

- B2HT54_MYCMM

UniProt

B2HT54 - B2HT54_MYCMM

Protein

Fumarate hydratase class II

Gene

fum

Organism
Mycobacterium marinum (strain ATCC BAA-535 / M)
Status
Unreviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (10 Jun 2008)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111SubstrateUniRule annotation

    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

    LyaseUniRule annotationSAAS annotation

    Keywords - Biological processi

    Tricarboxylic acid cycleUniRule annotation

    Enzyme and pathway databases

    BioCyciMMAR216594:GJOB-4401-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:fumImported
    Synonyms:fumCUniRule annotation
    Ordered Locus Names:MMAR_4368Imported
    OrganismiMycobacterium marinum (strain ATCC BAA-535 / M)Imported
    Taxonomic identifieri216594 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
    ProteomesiUP000001190: Chromosome

    Subcellular locationi

    Cytoplasm UniRule annotationSAAS annotation

    GO - Cellular componenti

    1. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    CytoplasmUniRule annotation

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi216594.MMAR_4368.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QBPX-ray1.85A/B/C/D1-474[»]
    ProteinModelPortaliB2HT54.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiB2HT54.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni133 – 1364B siteUniRule annotation
    Regioni143 – 1453Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061737.
    KOiK01679.
    OMAiENYRIES.
    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.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B2HT54-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAHSAHDDAD NDTEYRIEHD TMGEVRVPAK ALWRAQTQRA VENFPISGRG    50
    LERAQIRALG LLKGACAQVN MDLGLLAPEK AEAIIAAAAE IADGQHDDQF 100
    PIDVFQTGSG TSSNMNTNEV IASIAGANGV AVHPNDDVNM SQSSNDTFPT 150
    ATHIAATEAA VSHLIPALEI LQDALATKAL EWQSVVKSGR THLMDAVPVT 200
    LGQEFSGYAR QIEAGIERVR ATLPRLGELA IGGTAVGTGL NAPEGFGVKV 250
    VSVLVSQTGL PQLRTAANSF EAQAARDGLV EASGALRTIA VSLTKIANDI 300
    RWMGSGPLTG LAEIQLPDLQ PGSSIMPGKV NPVLPEAVTQ VAAQVIGNDA 350
    AVAWGGANGA FELNVYIPMM ARNILESFTL LTNVSKLFAQ RCIAGLTANA 400
    EHLRELAESS PSIVTPLNSA IGYEEAAAVA KQALKERKTI RQTVIDRGLI 450
    GDKLSLEELD RRLDVLAMAK VEATDD 476
    Length:476
    Mass (Da):50,192
    Last modified:June 10, 2008 - v1
    Checksum:iEA3DEA92B5FFD49F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000854 Genomic DNA. Translation: ACC42775.1.
    RefSeqiYP_001852630.1. NC_010612.1.

    Genome annotation databases

    EnsemblBacteriaiACC42775; ACC42775; MMAR_4368.
    GeneIDi6228650.
    KEGGimmi:MMAR_4368.
    PATRICi18070061. VBIMycMar75906_4696.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000854 Genomic DNA. Translation: ACC42775.1 .
    RefSeqi YP_001852630.1. NC_010612.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QBP X-ray 1.85 A/B/C/D 1-474 [» ]
    ProteinModelPortali B2HT54.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 216594.MMAR_4368.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ACC42775 ; ACC42775 ; MMAR_4368 .
    GeneIDi 6228650.
    KEGGi mmi:MMAR_4368.
    PATRICi 18070061. VBIMycMar75906_4696.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061737.
    KOi K01679.
    OMAi ENYRIES.
    OrthoDBi EOG6V1M4M.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci MMAR216594:GJOB-4401-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei B2HT54.

    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.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-535 / MImported.
    2. "Crystal structure of fumarase Fum from Mycobacterium marinum."
      Edwards T.E., Gardberg A.S., Sankaran B.
      Submitted (JAN-2011) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-474.

    Entry informationi

    Entry nameiB2HT54_MYCMM
    AccessioniPrimary (citable) accession number: B2HT54
    Entry historyi
    Integrated into UniProtKB/TrEMBL: June 10, 2008
    Last sequence update: June 10, 2008
    Last modified: October 1, 2014
    This is version 43 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    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.UniRule annotation

    Keywords - Technical termi

    3D-structureImported, Complete proteome, Reference proteomeImported

    External Data

    Dasty 3