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O94552

- FUMH_SCHPO

UniProt

O94552 - FUMH_SCHPO

Protein

Fumarate hydratase, mitochondrial

Gene

fum1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 3 (22 Sep 2009)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei155 – 1551SubstrateBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: PomBase

    GO - Biological processi

    1. fumarate metabolic process Source: PomBase
    2. tricarboxylic acid cycle Source: PomBase

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    ReactomeiREACT_213505. Citric acid cycle (TCA cycle).
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase, mitochondrial (EC:4.2.1.2)
    Short name:
    Fumarase
    Gene namesi
    Name:fum1
    ORF Names:SPCC18.18c, SPCC290.01c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome III

    Organism-specific databases

    PomBaseiSPCC18.18c.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: PomBase
    2. mitochondrial matrix Source: PomBase
    3. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3939MitochondrionSequence AnalysisAdd
    BLAST
    Chaini40 – 520481Fumarate hydratase, mitochondrialPRO_0000010332Add
    BLAST

    Proteomic databases

    MaxQBiO94552.
    PaxDbiO94552.

    Interactioni

    Protein-protein interaction databases

    BioGridi275911. 1 interaction.
    MINTiMINT-4685155.
    STRINGi4896.SPCC18.18c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO94552.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni184 – 1874B siteBy similarity
    Regioni194 – 1963Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    KOiK01679.
    OMAiMFSGPMT.
    OrthoDBiEOG73NGC9.
    PhylomeDBiO94552.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O94552-1 [UniParc]FASTAAdd to Basket

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    MASVAHISTA KAIFRAGGLP CRRLITPTLT GLPLKTHRMN STTPTYHLIP    50
    KGGKHGEFRQ ESDTFGPIQV PAEKYWGAQT QRSLQNFRIG GEKERLPLPL 100
    VRAFGVLKRA AASVNREFGL DPKLADAIEQ AAQEVIDGRL DDNFPLVVFQ 150
    TGSGTQSNMN SNEVIANRAI EILGGTLGSK KPVHPNDHVN MSQSSNDTFP 200
    TVMHIASVLQ IHTHLLPAMK HLHRALKGKE EEFKNIIKIG RTHMQDATPL 250
    SLGQEFSGYV TQVGYGIERI NNALPRLCLL AQGGTAVGTG LNTFEGFDVK 300
    VAEKVSKLTN IEFKTAPNKF EALAAHDAIV EMSGALNVIA CSLMKIANDI 350
    RQLGSGPRCG LGELILPANE PGSSIMPGKV NPTQCEALTM VCAQVMGNHA 400
    TITVAGASGH CELNVFKPLL AKNILSSIRL LGDACESFTD HCVVGIEPNY 450
    EGIARHLRDS LMLVTALNPH IGYDNCAKIA KTALKNKSTL KHEFVTLGFG 500
    TPEQFDEWVR PELMISAKKV 520
    Length:520
    Mass (Da):56,322
    Last modified:September 22, 2009 - v3
    Checksum:i4AF0DA8BF5E14AE8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329672 Genomic DNA. Translation: CAA21432.3.
    PIRiT41265.
    RefSeqiNP_588397.3. NM_001023388.3.

    Genome annotation databases

    EnsemblFungiiSPCC18.18c.1; SPCC18.18c.1:pep; SPCC18.18c.
    GeneIDi2539345.
    KEGGispo:SPCC18.18c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329672 Genomic DNA. Translation: CAA21432.3 .
    PIRi T41265.
    RefSeqi NP_588397.3. NM_001023388.3.

    3D structure databases

    ProteinModelPortali O94552.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 275911. 1 interaction.
    MINTi MINT-4685155.
    STRINGi 4896.SPCC18.18c-1.

    Proteomic databases

    MaxQBi O94552.
    PaxDbi O94552.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPCC18.18c.1 ; SPCC18.18c.1:pep ; SPCC18.18c .
    GeneIDi 2539345.
    KEGGi spo:SPCC18.18c.

    Organism-specific databases

    PomBasei SPCC18.18c.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    KOi K01679.
    OMAi MFSGPMT.
    OrthoDBi EOG73NGC9.
    PhylomeDBi O94552.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    Reactomei REACT_213505. Citric acid cycle (TCA cycle).

    Miscellaneous databases

    NextBioi 20800510.
    PROi O94552.

    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. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.

    Entry informationi

    Entry nameiFUMH_SCHPO
    AccessioniPrimary (citable) accession number: O94552
    Secondary accession number(s): O74868
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2003
    Last sequence update: September 22, 2009
    Last modified: October 1, 2014
    This is version 98 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3