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P10173

- FUMH_PIG

UniProt

P10173 - FUMH_PIG

Protein

Fumarate hydratase, mitochondrial

Gene

FH

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031SubstrateBy 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
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    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
    Chaini1 – 466466Fumarate hydratase, mitochondrialPRO_0000161335Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
    Modified residuei17 – 171N6-succinyllysine; alternateBy similarity
    Modified residuei22 – 221N6-acetyllysine; alternateBy similarity
    Modified residuei22 – 221N6-succinyllysine; alternateBy similarity
    Modified residuei36 – 361N6-acetyllysine; alternateBy similarity
    Modified residuei36 – 361N6-succinyllysine; alternateBy similarity
    Modified residuei50 – 501N6-acetyllysineBy similarity
    Modified residuei71 – 711N6-acetyllysine; alternateBy similarity
    Modified residuei71 – 711N6-succinyllysine; alternateBy similarity
    Modified residuei78 – 781N6-acetyllysine; alternateBy similarity
    Modified residuei78 – 781N6-succinyllysine; alternateBy similarity
    Modified residuei169 – 1691N6-acetyllysineBy similarity
    Modified residuei212 – 2121N6-acetyllysineBy similarity
    Modified residuei248 – 2481N6-acetyllysine; alternateBy similarity
    Modified residuei248 – 2481N6-succinyllysine; alternateBy similarity
    Modified residuei423 – 4231N6-succinyllysineBy similarity
    Modified residuei429 – 4291N6-succinyllysineBy similarity
    Modified residuei458 – 4581N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiP10173.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    3D structure databases

    ProteinModelPortaliP10173.
    SMRiP10173. Positions 5-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni132 – 1354B siteBy similarity
    Regioni142 – 1443Substrate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG002183.

    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.

    P10173-1 [UniParc]FASTAAdd to Basket

    « Hide

    ASQDSFRIEY DTFGELKVPN DKYYGAQTVR STMNFKIGGV TERMPIPVLK    50
    AFGILKRAAA EVNQDYGLDP KIANAIMKAA DEVAEGKLND HFPLVVWQTG 100
    SGTQTNMNVN EVISNRAIEM LGGELGSKKP VHPNDHVNKS QSSNDTFPTA 150
    MHIAAAVEVH EALLPGLQKL HDALDAKSRE FAQIIKIGRT HTQDAVPLTL 200
    GQEFSGYVQQ VKYAITRIKA AMPRIYELAA GGTAVGTGLN TRIGFAEKVA 250
    AKVAALTGLP FVTAPNNFEA LAAHDALVEH SGAMNTTACS LMKIANDIRF 300
    LGSGPRSGLG ELILPENEPG SSIMPGKVNP TQCEALTMVA AQVMGNHVAV 350
    TVGGSNGHFE LNVFKPMMIK NVLHSARLLG DAAVSFTENC VVGIQANTER 400
    INKLMNESLM LVTALNPHIG YDKAAKIAKT AHKNGSTLKA TAVELGYLTA 450
    EQFDEWVKPR DMLGPK 466
    Length:466
    Mass (Da):50,009
    Last modified:July 1, 1989 - v1
    Checksum:iE89F349D78FD98DC
    GO

    Sequence databases

    PIRiA27657. UFPG.

    Cross-referencesi

    Sequence databases

    PIRi A27657. UFPG.

    3D structure databases

    ProteinModelPortali P10173.
    SMRi P10173. Positions 5-466.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P10173.
    ChEMBLi CHEMBL6143.

    Proteomic databases

    PRIDEi P10173.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG002183.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .

    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: PROTEIN SEQUENCE.
      Tissue: Heart.

    Entry informationi

    Entry nameiFUMH_PIG
    AccessioniPrimary (citable) accession number: P10173
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 92 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, 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