Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O69294

- FUMC_CAMJE

UniProt

O69294 - FUMC_CAMJE

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei187 – 1871Proton donor/acceptorBy similarity
    Active sitei317 – 3171By similarity
    Binding sitei318 – 3181SubstrateUniRule annotation
    Sitei330 – 3301Important 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

    BioCyciCJEJ192222:GJTS-1337-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:Cj1364c
    OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
    Taxonomic identifieri192222 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
    ProteomesiUP000000799: 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_0000161263Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    IntActiO69294. 10 interactions.
    STRINGi192222.Cj1364c.

    Structurei

    3D structure databases

    ProteinModelPortaliO69294.
    SMRiO69294. Positions 4-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 993Substrate bindingUniRule annotation
    Regioni128 – 1314B siteUniRule annotation
    Regioni138 – 1403Substrate bindingUniRule annotation
    Regioni186 – 1872Substrate bindingUniRule annotation
    Regioni323 – 3253Substrate 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.

    O69294-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEYRVEHDTM GEVKVPNDKY WGAQTERSFE NFKIGCEKMP KVLIYAFANL    50
    KKSLALVNNK LGKLDDAKKN AIVQACDEII AGKFDDNFPL AIWQTGSGTQ 100
    SNMNMNEVIA NRATEIMGGD FRKEKLVHPN DHVNMSQSSN DTFPTAMSIV 150
    AVEQVEKKLI PALDELIATF EKKVKEFDGI IKIGRTHLQD ATPLTLAQEF 200
    SGYLSMLLHS KEQIIASLPT LRELAIGGTA VGTGLNAHPE LSQKVSEELT 250
    QLIGTKFISS PNKFHALTSH DAINFTHGAM KGLAANLMKI ANDIRWLASG 300
    PRCGLGELII PENEPGSSIM PGKVNPTQCE AVTMVAVQVM GNDVAIGFAA 350
    SQGNFELNVF KPVIIYNFLQ SLDLLADSMH SFNIHCAVGI EPNRAKIDHN 400
    LHNSLMLVTA LNPHIGYENA AKVAKNAHKK GISLKESTME LGLVSEEDFN 450
    KFVDPTKMIG PKA 463
    Length:463
    Mass (Da):50,710
    Last modified:August 1, 1998 - v1
    Checksum:iE281B37B5791FFC0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16882 Genomic DNA. Translation: CAA76499.1.
    AL111168 Genomic DNA. Translation: CAL35476.1.
    PIRiA81281.
    RefSeqiWP_002857888.1. NC_002163.1.
    YP_002344752.1. NC_002163.1.

    Genome annotation databases

    EnsemblBacteriaiCAL35476; CAL35476; Cj1364c.
    GeneIDi905657.
    KEGGicje:Cj1364c.
    PATRICi20059693. VBICamJej33762_1345.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y16882 Genomic DNA. Translation: CAA76499.1 .
    AL111168 Genomic DNA. Translation: CAL35476.1 .
    PIRi A81281.
    RefSeqi WP_002857888.1. NC_002163.1.
    YP_002344752.1. NC_002163.1.

    3D structure databases

    ProteinModelPortali O69294.
    SMRi O69294. Positions 4-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi O69294. 10 interactions.
    STRINGi 192222.Cj1364c.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL35476 ; CAL35476 ; Cj1364c .
    GeneIDi 905657.
    KEGGi cje:Cj1364c.
    PATRICi 20059693. VBICamJej33762_1345.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci CJEJ192222:GJTS-1337-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. Griffiths P.L., Connerton I.F.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NCTC 11168.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NCTC 11168.

    Entry informationi

    Entry nameiFUMC_CAMJE
    AccessioniPrimary (citable) accession number: O69294
    Secondary accession number(s): Q0P8P5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 101 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