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Q92PB6

- FUMC_RHIME

UniProt

Q92PB6 - FUMC_RHIME

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 2 (15 Dec 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei188 – 1881Proton donor/acceptorBy similarity
    Active sitei318 – 3181By similarity
    Binding sitei319 – 3191SubstrateBy similarity
    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

    BioCyciRETL1328306-WGS:GSTH-2397-MONOMER.
    SMEL266834:GJF6-1907-MONOMER.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase class II (EC:4.2.1.2)
    Short name:
    Fumarase C
    Gene namesi
    Name:fumC
    Ordered Locus Names:R01859
    ORF Names:SMc00149
    OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
    Taxonomic identifieri266834 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
    ProteomesiUP000001976: Chromosome

    Subcellular locationi

    Cytoplasm By similarity

    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_0000161305Add
    BLAST

    Proteomic databases

    ProMEXiQ92PB6.

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi266834.SMc00149.

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 96
    Beta strandi12 – 176
    Helixi24 – 329
    Helixi42 – 6120
    Helixi67 – 8115
    Helixi86 – 883
    Beta strandi92 – 954
    Helixi100 – 11718
    Turni122 – 1254
    Helixi130 – 1345
    Turni135 – 1373
    Helixi140 – 15819
    Helixi160 – 17819
    Beta strandi182 – 1876
    Beta strandi190 – 1967
    Helixi197 – 21721
    Helixi219 – 2224
    Turni230 – 2323
    Helixi242 – 25413
    Helixi264 – 2696
    Helixi272 – 29827
    Beta strandi302 – 3054
    Helixi328 – 35225
    Helixi362 – 38625
    Helixi388 – 3903
    Helixi395 – 40410
    Helixi407 – 4115
    Helixi413 – 4164
    Helixi418 – 43114
    Helixi435 – 4406
    Turni441 – 4433
    Helixi447 – 4537
    Helixi456 – 4583
    Beta strandi459 – 4613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HGVX-ray2.09A/B/C/D1-463[»]
    ProteinModelPortaliQ92PB6.
    SMRiQ92PB6. Positions 5-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 1003Substrate bindingBy similarity
    Regioni129 – 1324B siteBy similarity
    Regioni139 – 1413Substrate bindingBy similarity
    Regioni187 – 1882Substrate bindingBy similarity
    Regioni324 – 3263Substrate bindingBy similarity

    Sequence similaritiesi

    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.

    Q92PB6-1 [UniParc]FASTAAdd to Basket

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    MTSTRTETDT FGPIEVASDR YWGAQAQRSL GNFKIGWEKQ PLAIVRALGI    50
    VKQAAARANM ALGRLDPAIG DAIVKAAQEV IDGKLDEHFP LVVWQTGSGT 100
    QSNMNANEVV SNRAIELLGG VMGSKKPVHP NDHVNMSQSS NDTYPTAMHI 150
    ACAERVIHDL LPALKHLHKA LEEKVKAFDH IIKIGRTHTQ DATPLTLGQE 200
    FSGYAAQVAS SIKRIEMTLP GLCELAQGGT AVGTGLNAPV GFAEKVAEEI 250
    AAITGIGFTS APNKFEALAA HDSMVFSHGA INATAAALFK IANDIRFLGS 300
    GPRSGLGELS LPENEPGSSI MPGKVNPTQC EALTQVCVQV FGNHAALTFA 350
    GSQGHFELNV YNPLMAYNFL QSVQLLADAA ISFTDNCVVG IEAREDNIKA 400
    ALDRSLMLVT ALAPKIGYDN AAKIAKTAHK NGTTLREEAV GGGYVTDEEF 450
    DAVVRPETMI GPA 463
    Length:463
    Mass (Da):49,133
    Last modified:December 15, 2003 - v2
    Checksum:iA500EDE8A6789C5F
    GO

    Sequence cautioni

    The sequence CAC46438.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL591688 Genomic DNA. Translation: CAC46438.1. Different initiation.
    RefSeqiNP_385965.3. NC_003047.1.

    Genome annotation databases

    EnsemblBacteriaiCAC46438; CAC46438; SMc00149.
    GeneIDi1233524.
    KEGGisme:SMc00149.
    PATRICi23633127. VBISinMel96828_3302.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL591688 Genomic DNA. Translation: CAC46438.1 . Different initiation.
    RefSeqi NP_385965.3. NC_003047.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HGV X-ray 2.09 A/B/C/D 1-463 [» ]
    ProteinModelPortali Q92PB6.
    SMRi Q92PB6. Positions 5-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266834.SMc00149.

    Proteomic databases

    ProMEXi Q92PB6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAC46438 ; CAC46438 ; SMc00149 .
    GeneIDi 1233524.
    KEGGi sme:SMc00149.
    PATRICi 23633127. VBISinMel96828_3302.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci RETL1328306-WGS:GSTH-2397-MONOMER.
    SMEL266834:GJF6-1907-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1021.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 1021.
    3. Cited for: X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS), SUBUNIT.

    Entry informationi

    Entry nameiFUMC_RHIME
    AccessioniPrimary (citable) accession number: Q92PB6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 82 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3