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Q54VA2

- FUMH_DICDI

UniProt

Q54VA2 - FUMH_DICDI

Protein

Fumarate hydratase, mitochondrial

Gene

fumH

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei120 – 1201SubstrateBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: dictyBase

    GO - Biological processi

    1. fumarate metabolic process Source: dictyBase
    2. response to bacterium Source: dictyBase
    3. tricarboxylic acid cycle Source: dictyBase

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase, mitochondrial (EC:4.2.1.2)
    Short name:
    Fumarase
    Gene namesi
    Name:fumH
    ORF Names:DDB_G0280495
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 3, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0280495. fumH.

    Subcellular locationi

    Isoform 1 : Mitochondrion By similarity
    Isoform 2 : Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: dictyBase
    2. mitochondrion Source: dictyBase
    3. phagocytic vesicle Source: dictyBase
    4. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1919MitochondrionSequence AnalysisAdd
    BLAST
    Chaini20 – 485466Fumarate hydratase, mitochondrialPRO_0000331360Add
    BLAST

    Proteomic databases

    PRIDEiQ54VA2.

    Interactioni

    Protein-protein interaction databases

    STRINGi44689.DDB_0231397.

    Structurei

    3D structure databases

    ProteinModelPortaliQ54VA2.
    SMRiQ54VA2. Positions 23-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni150 – 1534B siteBy similarity
    Regioni160 – 1623Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0114.
    KOiK01679.
    OMAiMESFNIH.
    PhylomeDBiQ54VA2.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q54VA2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLSASRKLNN QQFLKTIRNM TTFRSEFDTF GEVKVNDEKY WGAQTQRSLE    50
    NFDIGGESEK MPLMVVRSFG ILKRCAAIVN KKYGLDATIA DNIAKAATEV 100
    VEGKLDDQFP LVVFQTGSGT QSNMNANEVI SNRAIELMTG KRDFSKKLVH 150
    PNDHVNKSQS SNDTFPTCMH IAAAISINEK LVPALEMLLA AMRTKQNEFN 200
    HIIKIGRTHL QDATPLTLGQ EFSGYCTQIE YGIQRIKDTL PRLYNLAQGG 250
    TAVGTGLNTP VGFDVDIASE VAKFTGLPFK TAPNKFEALA AHDAMVEVSG 300
    ALNTVAVSLM KIANDIRFLG SGPRCGLGEL ILPENEPGSS IMPGKVNPTQ 350
    CEAMTMVCAQ VMGNNTTVSI AGSNGHFELN VFKPVIIKNV LSSIRLIADA 400
    SVSFTKHCVV GIKADEKRID QLLHESLMLV TALNPYIGYD KAAKAAKKAH 450
    KEKTTLKEAC LSLGFTTSEE FDKWVDPSKM IGSMK 485
    Length:485
    Mass (Da):52,963
    Last modified:May 24, 2005 - v1
    Checksum:iA70941925A48FBBE
    GO
    Isoform 2 (identifier: Q54VA2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-19: Missing.

    Show »
    Length:466
    Mass (Da):50,718
    Checksum:iF428A15A5F9FB22B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1919Missing in isoform 2. CuratedVSP_033185Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000036 Genomic DNA. Translation: EAL67226.1.
    AAFI02000036 Genomic DNA. Translation: EAL67227.1.
    RefSeqiXP_001134561.1. XM_001134561.1.
    XP_641207.1. XM_636115.1.

    Genome annotation databases

    EnsemblProtistsiDDB0231397; DDB0231397; DDB_G0280495. [Q54VA2-1]
    GeneIDi8622588.
    KEGGiddi:DDB_G0280495.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFI02000036 Genomic DNA. Translation: EAL67226.1 .
    AAFI02000036 Genomic DNA. Translation: EAL67227.1 .
    RefSeqi XP_001134561.1. XM_001134561.1.
    XP_641207.1. XM_636115.1.

    3D structure databases

    ProteinModelPortali Q54VA2.
    SMRi Q54VA2. Positions 23-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0231397.

    Proteomic databases

    PRIDEi Q54VA2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0231397 ; DDB0231397 ; DDB_G0280495 . [Q54VA2-1 ]
    GeneIDi 8622588.
    KEGGi ddi:DDB_G0280495.

    Organism-specific databases

    dictyBasei DDB_G0280495. fumH.

    Phylogenomic databases

    eggNOGi COG0114.
    KOi K01679.
    OMAi MESFNIH.
    PhylomeDBi Q54VA2.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    Miscellaneous databases

    PROi Q54VA2.

    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 of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.

    Entry informationi

    Entry nameiFUMH_DICDI
    AccessioniPrimary (citable) accession number: Q54VA2
    Secondary accession number(s): Q54VA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3