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P28894

- FUMC1_BRADU

UniProt

P28894 - FUMC1_BRADU

Protein

Fumarate hydratase class II 1

Gene

fumC1

Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 3 (15 Dec 2003)
      Previous versions | rss
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    • 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 sitei198 – 1981Proton donor/acceptorBy similarity
    Active sitei328 – 3281By similarity
    Binding sitei329 – 3291SubstrateUniRule annotation
    Sitei341 – 3411Important 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

    BioCyciBJAP224911:GJEJ-6569-MONOMER.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase class II 1UniRule annotation (EC:4.2.1.2UniRule annotation)
    Short name:
    Fumarase C 1UniRule annotation
    Gene namesi
    Name:fumC1UniRule annotation
    Synonyms:fumC
    Ordered Locus Names:blr6519
    OrganismiBradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
    Taxonomic identifieri224911 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium
    ProteomesiUP000002526: Chromosome

    Subcellular locationi

    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 – 473473Fumarate hydratase class II 1PRO_0000161259Add
    BLAST

    Proteomic databases

    PRIDEiP28894.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Protein-protein interaction databases

    STRINGi224911.blr6519.

    Structurei

    3D structure databases

    ProteinModelPortaliP28894.
    SMRiP28894. Positions 15-472.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni108 – 1103Substrate bindingUniRule annotation
    Regioni139 – 1424B siteUniRule annotation
    Regioni149 – 1513Substrate bindingUniRule annotation
    Regioni197 – 1982Substrate bindingUniRule annotation
    Regioni334 – 3363Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    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.

    P28894-1 [UniParc]FASTAAdd to Basket

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    MAKSARTKTA RPATRTETDS FGPIEVPSDR YWGAQTERSR QNFRIGTDRM    50
    PISLVHALGI VKLAAAQSNR ELGLLDQRRA SAIIRAAREV IDGSLDDHFP 100
    LVVWQTGSGT QTNMNLNEVI ANRANELLGG ELGAKKPVHP NDHVNMSQSS 150
    NDSFPTAMHI AAASRITADL VPALGELLRA LRKKEKEFAK IVKIGRTHTQ 200
    DATPLTLGQE FSGYAAQVES GIARLKVAVK ELYPLAQGGT AVGTGLNAKP 250
    RFARLFAKHV AGITKLPFTS AANKFEALAS NDAYVLAHGA ISSVATGLFK 300
    IANDIRLLGS GPRSGLGELI LPENEPGSSI MPGKVNPTQC EAMTMVCCQV 350
    FGNHTAITVA GSQGHFELNV YKPVLAYNML HSIRLMADAA RSFTEHCVSG 400
    IRADEKRISE LMQRSLMLVT ALAPKIGYDN AAKVAKTAHA NGTTLKEEAL 450
    RLGFVTADEF DRLVQPEKMT KPG 473
    Length:473
    Mass (Da):50,924
    Last modified:December 15, 2003 - v3
    Checksum:iCDB35CFA32062957
    GO

    Sequence cautioni

    The sequence AAA26211.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAC51784.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 944IDGS → STAD in AAA26211. (PubMed:1856685)Curated
    Sequence conflicti91 – 944IDGS → STAD in AAA26212. (PubMed:1856685)Curated
    Sequence conflicti220 – 2201S → R in AAA26211. (PubMed:1856685)Curated
    Sequence conflicti220 – 2201S → R in AAA26212. (PubMed:1856685)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M79457 Genomic DNA. Translation: AAA26211.1. Different initiation.
    M79457 Genomic DNA. Translation: AAA26212.1.
    BA000040 Genomic DNA. Translation: BAC51784.1. Different initiation.
    RefSeqiNP_773159.2. NC_004463.1.

    Genome annotation databases

    EnsemblBacteriaiBAC51784; BAC51784; BAC51784.
    GeneIDi1054478.
    KEGGibja:blr6519.
    PATRICi21196868. VBIBraJap65052_6668.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M79457 Genomic DNA. Translation: AAA26211.1 . Different initiation.
    M79457 Genomic DNA. Translation: AAA26212.1 .
    BA000040 Genomic DNA. Translation: BAC51784.1 . Different initiation.
    RefSeqi NP_773159.2. NC_004463.1.

    3D structure databases

    ProteinModelPortali P28894.
    SMRi P28894. Positions 15-472.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224911.blr6519.

    Proteomic databases

    PRIDEi P28894.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAC51784 ; BAC51784 ; BAC51784 .
    GeneIDi 1054478.
    KEGGi bja:blr6519.
    PATRICi 21196868. VBIBraJap65052_6668.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci BJAP224911:GJEJ-6569-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. "Cloning, sequencing, and mutational analysis of the Bradyrhizobium japonicum fumC-like gene: evidence for the existence of two different fumarases."
      Acuna G., Ebeling S., Hennecke H.
      J. Gen. Microbiol. 137:991-1000(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: USDA 110spc4.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110.

    Entry informationi

    Entry nameiFUMC1_BRADU
    AccessioniPrimary (citable) accession number: P28894
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 103 of the entry and version 3 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