Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8F9L0

- FUMC_LEPIN

UniProt

Q8F9L0 - FUMC_LEPIN

Protein

Fumarate hydratase class II

Gene

fumC

Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
    • Help video
    • Feedback
    • 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 sitei187 – 1871Proton donor/acceptorBy similarity
    Active sitei317 – 3171By similarity
    Binding sitei318 – 3181SubstrateUniRule annotation
    Sitei330 – 3301Important 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

    BioCyciLINT189518:GJBB-158-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:fum
    Ordered Locus Names:LA_0185
    OrganismiLeptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
    Taxonomic identifieri189518 [NCBI]
    Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesLeptospiraceaeLeptospira
    ProteomesiUP000001408: Chromosome I

    Subcellular locationi

    Cytoplasm UniRule annotation

    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 – 464464Fumarate hydratase class IIPRO_0000161283Add
    BLAST

    Proteomic databases

    PaxDbiQ8F9L0.

    Interactioni

    Subunit structurei

    Homotetramer.UniRule annotation

    Structurei

    3D structure databases

    ProteinModelPortaliQ8F9L0.
    SMRiQ8F9L0. Positions 4-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni97 – 993Substrate bindingUniRule annotation
    Regioni128 – 1314B siteUniRule annotation
    Regioni138 – 1403Substrate bindingUniRule annotation
    Regioni186 – 1872Substrate bindingUniRule annotation
    Regioni323 – 3253Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiMESFNIH.
    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.

    Q8F9L0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKTRIETDSM GEIAVDDSKY WGAQTERSLH HFHIGNDRFP REMIRALGIL    50
    KKSAAVVNAE LGLLSEDKKK LIVQAADEVI SGKLDEHFPL SVWQTGSGTQ 100
    TNMNSNEVIS NRAIEIAGGV KGSKKPIHPN DDVNKAQSSN DTFPTAMHIA 150
    AAEQLNQKLI PALIQLKETF KKKTDEFQNI IKIGRTHLQD ATPLTLGQEF 200
    SGYVQQLEYN IARVKAVLPS VYRLALGGTA VGTGLNTHPQ FAVKAAAQIA 250
    KETGLPFVSA ENKFEALAAH DSLVETSGVL KTIAASLMKI ANDIRWLSSG 300
    PRCGIGEISI PENEPGSSIM PGKVNPTQSE QMTMVAAQVI ANDVAVNIGG 350
    ASGNFELNVF KPLIIHNVLN SIRLLSDSCV SFEEHCARGI IPNKEKLNEH 400
    LNNSLMLVTA LNPHIGYDNA AKIAKNAHKK GTTLKESGIE LGLLTSEQFD 450
    QWVLPEKMIH PSVD 464
    Length:464
    Mass (Da):50,397
    Last modified:March 1, 2003 - v1
    Checksum:iAE316E36BAB02FA8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010300 Genomic DNA. Translation: AAN47384.1.
    AB010203 Genomic DNA. Translation: BAA24376.1.
    PIRiT00129.
    RefSeqiNP_710366.1. NC_004342.2.

    Genome annotation databases

    EnsemblBacteriaiAAN47384; AAN47384; LA_0185.
    GeneIDi1149528.
    KEGGilil:LA_0185.
    PATRICi22381209. VBILepInt91350_0184.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE010300 Genomic DNA. Translation: AAN47384.1 .
    AB010203 Genomic DNA. Translation: BAA24376.1 .
    PIRi T00129.
    RefSeqi NP_710366.1. NC_004342.2.

    3D structure databases

    ProteinModelPortali Q8F9L0.
    SMRi Q8F9L0. Positions 4-459.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi Q8F9L0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAN47384 ; AAN47384 ; LA_0185 .
    GeneIDi 1149528.
    KEGGi lil:LA_0185.
    PATRICi 22381209. VBILepInt91350_0184.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    BioCyci LINT189518:GJBB-158-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: 56601.
    2. "Physical and genetic maps of the Leptospira interrogans serovar icterohaemorrhagiae strain Ictero No.1 chromosome and sequencing of a 19-kb region of the genome containing the 5S rRNA gene."
      Takahashi Y., Akase K., Hirano H., Fukunaga M.
      Gene 215:37-45(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-459.
      Strain: Ictero No.1 / Serogroup Icterohaemorrhagiae.

    Entry informationi

    Entry nameiFUMC_LEPIN
    AccessioniPrimary (citable) accession number: Q8F9L0
    Secondary accession number(s): O50640
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 78 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

    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