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P39461

- FUMC_SULSO

UniProt

P39461 - FUMC_SULSO

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    May function as an auxiliary aerobic enzyme in the citric acid cycle.1 Publication

    Catalytic activityi

    (S)-malate = fumarate + H2O.1 Publication

    Kineticsi

    1. KM=0.125 mM for malate (at pH 7.5 and at 70 degrees Celsius)1 Publication
    2. KM=0.3 mM for malate (at pH 7.5 and at 70 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Temperature dependencei

    Optimum temperature is 85 degrees Celsius. Active from 40 to 90 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei160 – 1601Proton donor/acceptorBy similarity
    Active sitei291 – 2911By similarity
    Binding sitei292 – 2921SubstrateBy similarity
    Sitei304 – 3041Important 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

    BioCyciSSOL273057:GCH2-1024-MONOMER.
    BRENDAi4.2.1.2. 6163.
    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:SSO1077
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001974: 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 – 438438Fumarate hydratase class IIPRO_0000161334Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRINGi273057.SSO1077.

    Structurei

    3D structure databases

    ProteinModelPortaliP39461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni76 – 783Substrate bindingBy similarity
    Regioni101 – 1044B siteBy similarity
    Regioni111 – 1133Substrate bindingBy similarity
    Regioni159 – 1602Substrate bindingBy similarity
    Regioni297 – 2993Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiLEANEDH.

    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.
    IPR001611. Leu-rich_rpt.
    [Graphical view]
    PANTHERiPTHR11444. PTHR11444. 1 hit.
    PfamiPF10415. FumaraseC_C. 1 hit.
    PF00206. Lyase_1. 1 hit.
    [Graphical view]
    PRINTSiPR00149. FUMRATELYASE.
    SUPFAMiSSF48557. SSF48557. 1 hit.
    PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
    PS51450. LRR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39461-1 [UniParc]FASTAAdd to Basket

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    MKYTDTAPKL FMNTGTKFPR RIIWSMGVLK KSCAKVNADL GLLDKKIADS    50
    IIKASDDLID GKLDDKIVLD VFQTGSGTGL NMNVNEVIAE VASSYSNLKV 100
    HPNDHVNFGQ SSNDTVPTAI RIAAVAEVTN RLLPALQQII SSLNKKAEEY 150
    KDVIKAGRTH LRDALPVTLG QELSAYADAF QHEHEQVMNI LEYVKELPIG 200
    GTATGTGLNS HPEFQERVIN EINRITGLGF KPANRFRAMR LLTDLLLLSG 250
    ALRNIAVDLY RLGQDIRLMF SGPLTGLNEI DLPTQEEIAG SSIMPGKTNP 300
    VTVEATLLIS AQVVGLDHAN QFASMLGEFE LSMGIPLVGY NIVTQVNFIS 350
    EALEKMSRLV IDGMVANVEK MKRYAESSPS LITIVSPVIG YDKATEIGKK 400
    LNKGMSIREA LRELGYSDNE INKILDLSKL VKPGFTAK 438
    Length:438
    Mass (Da):47,911
    Last modified:February 1, 1995 - v1
    Checksum:i8D2A9CF37817EA6C
    GO

    Sequence cautioni

    The sequence AAK41339.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75402 Genomic DNA. Translation: CAA53156.1.
    AE006641 Genomic DNA. Translation: AAK41339.1. Different initiation.
    PIRiD90260.
    S40448.
    RefSeqiNP_342549.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK41339; AAK41339; SSO1077.
    GeneIDi1454118.
    KEGGisso:SSO1077.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75402 Genomic DNA. Translation: CAA53156.1 .
    AE006641 Genomic DNA. Translation: AAK41339.1 . Different initiation.
    PIRi D90260.
    S40448.
    RefSeqi NP_342549.1. NC_002754.1.

    3D structure databases

    ProteinModelPortali P39461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273057.SSO1077.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK41339 ; AAK41339 ; SSO1077 .
    GeneIDi 1454118.
    KEGGi sso:SSO1077.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi LEANEDH.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci SSOL273057:GCH2-1024-MONOMER.
    BRENDAi 4.2.1.2. 6163.

    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.
    IPR001611. Leu-rich_rpt.
    [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.
    PROSITEi PS00163. FUMARATE_LYASES. 1 hit.
    PS51450. LRR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, nucleotide sequence and expression of a Sulfolobus solfataricus gene encoding a class II fumarase."
      Colombo S., Grisa M., Tortora P., Vanoni M.
      FEBS Lett. 337:93-98(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-14.
      Strain: DSM 5833 / MT-4.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    3. "Purification and properties of a thermostable fumarate hydratase from the archaeobacterium Sulfolobus solfataricus."
      Puchegger S., Redl B., Stoeffler G.
      J. Gen. Microbiol. 136:1537-1541(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
      Strain: ATCC 35091 / DSM 1616 / IFO 15331 / JCM 8930 / P1.

    Entry informationi

    Entry nameiFUMC_SULSO
    AccessioniPrimary (citable) accession number: P39461
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 99 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

    Complete proteome, Direct protein sequencing, 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