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Q7SX99

- FUMH_DANRE

UniProt

Q7SX99 - FUMH_DANRE

Protein

Fumarate hydratase, mitochondrial

Gene

fh

Organism
Danio rerio (Zebrafish) (Brachydanio rerio)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei146 – 1461SubstrateBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: UniProtKB-EC

    GO - Biological processi

    1. fumarate metabolic process Source: InterPro
    2. tricarboxylic acid cycle Source: UniProtKB-UniPathway

    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:fh
    ORF Names:zgc:66253
    OrganismiDanio rerio (Zebrafish) (Brachydanio rerio)
    Taxonomic identifieri7955 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio
    ProteomesiUP000000437: Unplaced

    Organism-specific databases

    ZFINiZDB-GENE-010724-6. fh.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. tricarboxylic acid cycle enzyme complex Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4343MitochondrionBy similarityAdd
    BLAST
    Chaini44 – 509466Fumarate hydratase, mitochondrialPRO_0000010327Add
    BLAST

    Proteomic databases

    PRIDEiQ7SX99.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    STRINGi7955.ENSDARP00000097494.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7SX99.
    SMRiQ7SX99. Positions 48-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 1784B siteBy similarity
    Regioni185 – 1873Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    HOVERGENiHBG002183.
    KOiK01679.
    PhylomeDBiQ7SX99.

    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.

    Q7SX99-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRSARSLHR FSASLSDLRA AQRSIKARNV CPAPGLRHQT VRMASSEAFR    50
    IERDTFGELK VPSDKYYGAQ TVRSTMNFRI GGVTERMPIQ VIRAFGILKK 100
    AAAEVNKDYG LDPKIADAIM KAADEVESGK LDDHFPLVVW QTGSGTQTNM 150
    NVNEVISNRA IEMLGGKLGS KDPVHPNDHV NKSQSSNDTF PTAMHIAAAK 200
    EVHEVLLPGL QTLHDALAAK AEQFKDIIKI GRTHTQDAVP LSLGQEFGGY 250
    VQQVKYSIAR VKASLPRVYE LAAGGTAVGT GLNTRIGFAE KVADKVSALT 300
    GLPFVTAANK FEALAAHDAL VELSGALNTV AVSMMKIAND IRFLGSGPRS 350
    GLGELILPEN EPGSSIMPGK VNPTQCEAMT MVAAQVMGNH VAVTVGGSNG 400
    HFELNVFKPM IIKNVLNSAR LLGDASVSFT NNCVVGIEAN TERINKLMSE 450
    SLMLVTALNP HIGYDKAAKI AKTAHKDGST LKEAALKLGF LNEQQFEEWV 500
    RPHDMLGPK 509
    Length:509
    Mass (Da):54,861
    Last modified:October 1, 2003 - v1
    Checksum:i36A829D58EE18678
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC055566 mRNA. Translation: AAH55566.1.
    BC066484 mRNA. Translation: AAH66484.1.
    RefSeqiNP_957257.1. NM_200963.1.
    UniGeneiDr.104452.

    Genome annotation databases

    GeneIDi393938.
    KEGGidre:393938.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC055566 mRNA. Translation: AAH55566.1 .
    BC066484 mRNA. Translation: AAH66484.1 .
    RefSeqi NP_957257.1. NM_200963.1.
    UniGenei Dr.104452.

    3D structure databases

    ProteinModelPortali Q7SX99.
    SMRi Q7SX99. Positions 48-509.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 7955.ENSDARP00000097494.

    Proteomic databases

    PRIDEi Q7SX99.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 393938.
    KEGGi dre:393938.

    Organism-specific databases

    CTDi 2271.
    ZFINi ZDB-GENE-010724-6. fh.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    HOVERGENi HBG002183.
    KOi K01679.
    PhylomeDBi Q7SX99.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    Miscellaneous databases

    NextBioi 20814910.
    PROi Q7SX99.

    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. NIH - Zebrafish Gene Collection (ZGC) project
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: AB.
      Tissue: Kidney.

    Entry informationi

    Entry nameiFUMH_DANRE
    AccessioniPrimary (citable) accession number: Q7SX99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2003
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 84 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3