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P07343

- FUMC_BACSU

UniProt

P07343 - FUMC_BACSU

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      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 sitei186 – 1861Proton donor/acceptorBy similarity
    Active sitei316 – 3161By similarity
    Binding sitei317 – 3171SubstrateUniRule annotation
    Sitei329 – 3291Important 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

    BioCyciBSUB:BSU33040-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
    Synonyms:citG
    Ordered Locus Names:BSU33040
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU33040. [Micado]

    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 – 462462Fumarate hydratase class IIPRO_0000161255Add
    BLAST

    Proteomic databases

    PaxDbiP07343.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP07343. 2 interactions.
    MINTiMINT-8365703.
    STRINGi224308.BSU33040.

    Structurei

    3D structure databases

    ProteinModelPortaliP07343.
    SMRiP07343. Positions 4-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 993Substrate bindingUniRule annotation
    Regioni127 – 1304B siteUniRule annotation
    Regioni137 – 1393Substrate bindingUniRule annotation
    Regioni185 – 1862Substrate bindingUniRule annotation
    Regioni322 – 3243Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiMESFNIH.
    OrthoDBiEOG6V1M4M.
    PhylomeDBiP07343.

    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.

    P07343-1 [UniParc]FASTAAdd to Basket

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    MEYRIERDTM GEVKVPADKF WGAQTQRSKE NFKIGSEKMP MRVVKAFAIL    50
    KRSTALANKR LGNLDAEKAE AIAAVCDDVL KGKYDDNFPL VVWQTGSGTQ 100
    SNMNMNEVVA NRATALLKEK NSDQTIHPND DVNRSQSSND TFPTAMHVAA 150
    VLAVYEQLVP ALDQLRNTLD EKAKAYNDIV KIGRTHLQDA TPLTLGQEIS 200
    GWVHMLDRSK EMILEATDKM RALAIGGTAV GTGINAHPEF GELVSEEITK 250
    LTGQTFSSSP NKFHALTSHD EITYAHGALK ALAADLMKIA NDVRWLASGP 300
    RCGIGEIVIP ENEPGSSIMP GKVNPTQSEA LTMIAAQIMG NDATIGFAAS 350
    QGNFELNVFK PVIIYNFLQS VQLLSDGMNS FHDKCAVGIE PNKETIQENL 400
    SNSLMLVTAL NPHIGYENAA KIAKLAHKEG LTLKEAALKL ELLTEEQFNE 450
    MVKPEDMVKP KA 462
    Length:462
    Mass (Da):50,532
    Last modified:May 30, 2000 - v2
    Checksum:i8D797D18FEA82C06
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661A → V in CAA25849. (PubMed:3923430)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01701 Genomic DNA. Translation: CAA25849.1.
    AJ223978 Genomic DNA. Translation: CAA11749.1.
    AL009126 Genomic DNA. Translation: CAB15294.1.
    M11918 Genomic DNA. Translation: AAA22464.1.
    Z93941 Genomic DNA. Translation: CAB07973.1.
    PIRiA23033. UFBSC8.
    RefSeqiNP_391184.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB15294; CAB15294; BSU33040.
    GeneIDi938591.
    KEGGibsu:BSU33040.
    PATRICi18978594. VBIBacSub10457_3460.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01701 Genomic DNA. Translation: CAA25849.1 .
    AJ223978 Genomic DNA. Translation: CAA11749.1 .
    AL009126 Genomic DNA. Translation: CAB15294.1 .
    M11918 Genomic DNA. Translation: AAA22464.1 .
    Z93941 Genomic DNA. Translation: CAB07973.1 .
    PIRi A23033. UFBSC8.
    RefSeqi NP_391184.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P07343.
    SMRi P07343. Positions 4-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P07343. 2 interactions.
    MINTi MINT-8365703.
    STRINGi 224308.BSU33040.

    Proteomic databases

    PaxDbi P07343.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB15294 ; CAB15294 ; BSU33040 .
    GeneIDi 938591.
    KEGGi bsu:BSU33040.
    PATRICi 18978594. VBIBacSub10457_3460.

    Organism-specific databases

    GenoListi BSU33040. [Micado ]

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi MESFNIH.
    OrthoDBi EOG6V1M4M.
    PhylomeDBi P07343.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci BSUB:BSU33040-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. "Complete nucleotide sequence of the fumarase gene (citG) of Bacillus subtilis 168."
      Miles J.S., Guest J.R.
      Nucleic Acids Res. 13:131-140(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor."
      Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.
      Microbiology 144:1593-1600(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "The nucleotide sequence of a spore germination gene (gerA) of Bacillus subtilis 168."
      Feavers I.M., Miles J.S., Moir A.
      Gene 38:95-102(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
      Strain: 168.
    5. "Role of sigma H in expression of the fumarase gene (citG) in vegetative cells of Bacillus subtilis 168."
      Price V.A., Feavers I.M., Moir A.
      J. Bacteriol. 171:5933-5939(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
      Strain: 168.
    6. "Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis."
      Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.
      Microbiology 143:3305-3308(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 224-462.

    Entry informationi

    Entry nameiFUMC_BACSU
    AccessioniPrimary (citable) accession number: P07343
    Secondary accession number(s): O32194
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 118 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

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3