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Protein

Fumarate hydratase class II

Gene

fumC

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

    Pathway:itricarboxylic acid cycle

    This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from fumarate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Fumarate hydratase class II (fumC)
    This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-malate from fumarate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

    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

    GO - Biological processi

    Complete GO annotation...

    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 Componenti: Chromosome

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    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.
    InParanoidiP39461.
    KOiK01679.
    OMAiIEKDTMG.

    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

    « Hide

            10         20         30         40         50
    MKYTDTAPKL FMNTGTKFPR RIIWSMGVLK KSCAKVNADL GLLDKKIADS
    60 70 80 90 100
    IIKASDDLID GKLDDKIVLD VFQTGSGTGL NMNVNEVIAE VASSYSNLKV
    110 120 130 140 150
    HPNDHVNFGQ SSNDTVPTAI RIAAVAEVTN RLLPALQQII SSLNKKAEEY
    160 170 180 190 200
    KDVIKAGRTH LRDALPVTLG QELSAYADAF QHEHEQVMNI LEYVKELPIG
    210 220 230 240 250
    GTATGTGLNS HPEFQERVIN EINRITGLGF KPANRFRAMR LLTDLLLLSG
    260 270 280 290 300
    ALRNIAVDLY RLGQDIRLMF SGPLTGLNEI DLPTQEEIAG SSIMPGKTNP
    310 320 330 340 350
    VTVEATLLIS AQVVGLDHAN QFASMLGEFE LSMGIPLVGY NIVTQVNFIS
    360 370 380 390 400
    EALEKMSRLV IDGMVANVEK MKRYAESSPS LITIVSPVIG YDKATEIGKK
    410 420 430
    LNKGMSIREA LRELGYSDNE INKILDLSKL VKPGFTAK
    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.Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X75402 Genomic DNA. Translation: CAA53156.1.
    AE006641 Genomic DNA. Translation: AAK41339.1. Different initiation.
    PIRiD90260.
    S40448.
    RefSeqiNP_342549.1. NC_002754.1.

    3D structure databases

    ProteinModelPortaliP39461.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO1077.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    InParanoidiP39461.
    KOiK01679.
    OMAiIEKDTMG.

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER01007.
    BioCyciSSOL273057:GCH2-1024-MONOMER.
    BRENDAi4.2.1.2. 6163.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: July 22, 2015
    This is version 104 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.