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Q8DIP7

- FUMC_THEEB

UniProt

Q8DIP7 - FUMC_THEEB

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Thermosynechococcus elongatus (strain BP-1)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      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 sitei189 – 1891Proton donor/acceptorBy similarity
    Active sitei319 – 3191By similarity
    Binding sitei320 – 3201SubstrateUniRule annotation
    Sitei332 – 3321Important 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

    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:tll1534
    OrganismiThermosynechococcus elongatus (strain BP-1)
    Taxonomic identifieri197221 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus
    ProteomesiUP000000440: 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 – 467467Fumarate hydratase class IIPRO_0000161323Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi197221.tll1534.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8DIP7.
    SMRiQ8DIP7. Positions 6-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni99 – 1013Substrate bindingUniRule annotation
    Regioni130 – 1334B siteUniRule annotation
    Regioni140 – 1423Substrate bindingUniRule annotation
    Regioni188 – 1892Substrate bindingUniRule annotation
    Regioni325 – 3273Substrate 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.

    Q8DIP7-1 [UniParc]FASTAAdd to Basket

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    MTTDTRLEYD SLGAVEVPAD CYWGAQTARS LKHFAIGSQR MPLAVIHAMA    50
    RLKKAAAIAN RDLGVLDPEK AKWIIQAADE VIAGQWDDQF PLAIWQTGSG 100
    TQTNMNVNEV IANRAIELAG GVKGSKSPIH PNDHVNCSQS SNDTFPTAMH 150
    VATVLALQER LLPTLRHLLT VLQEKAAAFA EIIKIGRTHL MDAVPLTLGQ 200
    EFSGYASQIA AAQAHIEYAL QHLYPLAIGA TAVGTGLNAP AGFGDRVAAE 250
    LAQMTGYPFR KAENPFAALA AHDPLVMLSG ALKTLAAALM KIANDIRWLG 300
    SGPRCGLGEL RLPANEPGSS IMPGKVNPTQ CEALTMVCVQ VMGNDAAVGI 350
    AGSQGNFELN VYKPLIIYNV LQSIALLSDA AQSFTDHCLV GVEPNRQQIQ 400
    AYVERSLMLV TALNPHIGYD KAAAVAKKAY SEGKTLKEAA VELGYLTAEE 450
    FDRWVRLELM LGEKGTS 467
    Length:467
    Mass (Da):50,030
    Last modified:March 1, 2003 - v1
    Checksum:i79F600152E5C0D66
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC09086.1.
    RefSeqiNP_682324.1. NC_004113.1.

    Genome annotation databases

    EnsemblBacteriaiBAC09086; BAC09086; BAC09086.
    GeneIDi1011091.
    KEGGitel:tll1534.
    PATRICi23928428. VBITheElo119873_1609.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BA000039 Genomic DNA. Translation: BAC09086.1 .
    RefSeqi NP_682324.1. NC_004113.1.

    3D structure databases

    ProteinModelPortali Q8DIP7.
    SMRi Q8DIP7. Positions 6-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 197221.tll1534.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC09086 ; BAC09086 ; BAC09086 .
    GeneIDi 1011091.
    KEGGi tel:tll1534.
    PATRICi 23928428. VBITheElo119873_1609.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: BP-1.

    Entry informationi

    Entry nameiFUMC_THEEB
    AccessioniPrimary (citable) accession number: Q8DIP7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 77 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, 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