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Q60HF9

- FUMH_MACFA

UniProt

Q60HF9 - FUMH_MACFA

Protein

Fumarate hydratase, mitochondrial

Gene

FH

Organism
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 60 (01 Oct 2014)
      Sequence version 1 (23 Nov 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei147 – 1471SubstrateBy 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:QorA-13820
    OrganismiMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
    Taxonomic identifieri9541 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4444MitochondrionBy similarityAdd
    BLAST
    Chaini45 – 510466Fumarate hydratase, mitochondrialPRO_0000010321Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei61 – 611N6-acetyllysine; alternateBy similarity
    Modified residuei61 – 611N6-succinyllysine; alternateBy similarity
    Modified residuei66 – 661N6-acetyllysine; alternateBy similarity
    Modified residuei66 – 661N6-succinyllysine; alternateBy similarity
    Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
    Modified residuei80 – 801N6-succinyllysine; alternateBy similarity
    Modified residuei94 – 941N6-acetyllysineBy similarity
    Modified residuei115 – 1151N6-acetyllysine; alternateBy similarity
    Modified residuei115 – 1151N6-succinyllysine; alternateBy similarity
    Modified residuei122 – 1221N6-acetyllysine; alternateBy similarity
    Modified residuei122 – 1221N6-succinyllysine; alternateBy similarity
    Modified residuei213 – 2131N6-acetyllysineBy similarity
    Modified residuei223 – 2231N6-acetyllysine; alternateBy similarity
    Modified residuei223 – 2231N6-succinyllysine; alternateBy similarity
    Modified residuei256 – 2561N6-acetyllysineBy similarity
    Modified residuei292 – 2921N6-acetyllysine; alternateBy similarity
    Modified residuei292 – 2921N6-succinyllysine; alternateBy similarity
    Modified residuei467 – 4671N6-succinyllysineBy similarity
    Modified residuei473 – 4731N6-succinyllysineBy similarity
    Modified residuei502 – 5021N6-acetyllysineBy similarity

    Post-translational modificationi

    Isoform Cytoplasmic contains is acetylated at position 2.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ60HF9.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ60HF9.
    SMRiQ60HF9. Positions 49-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni176 – 1794B siteBy similarity
    Regioni186 – 1883Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    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]

    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 initiation. Align

    Isoform Mitochondrial (identifier: Q60HF9-1) [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

    MYRALWLLAR SRRLVRPPAS ALASAPGLSG AAVPSFWPPN AARMASQNSF    50
    RIEYDTFGEL KVPNDKYYGA QTVRSTMNFK IGGVTERMPT PVIKAFGILK 100
    RAAAEVNQDY GLDPKIANAI MKAADEVAEG KLNDHFPLVV WQTGSGTQTN 150
    MNVNEVISNR AIEMLGGELG SKIPVHPNDH VNKSQSSNDT FPTAMHIAAA 200
    IEVHEVLLPG LQKLHDALDA KSKEFAQIIK IGRTHTQDAV PLTLGQEFSG 250
    YVQQVKYAVT RIKAAMPRIY ELAAGGTAVG TGLNTRIGFA EKVAAKVAAL 300
    TGLPFVTAPN KFEALAAHDA LVELSGAMNT TACSLMKIAN DIRFLGSGPR 350
    SGLGELILPE NEPGSSIMPG KVNPTQCEAM TMVAAQVMGN HVAVTVGGSN 400
    GHFELNVFKP MMIKNVLHSA RLLGDASVSF TENCVVGIQA NTERINKLMN 450
    ESLMLVTALN PHIGYDKAAK IAKTAHKNGS TLKETAIELG YLTAEQFDEW 500
    VKPKDMLGPK 510
    Length:510
    Mass (Da):54,766
    Last modified:November 23, 2004 - v1
    Checksum:iF5FC970E977DEA09
    GO
    Isoform Cytoplasmic (identifier: Q60HF9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: Missing.

    Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2 (By similarity).By similarity

    Show »
    Length:467
    Mass (Da):50,181
    Checksum:i291AC7968C06254F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4343Missing in isoform Cytoplasmic. CuratedVSP_018966Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB125168 mRNA. Translation: BAD51956.1.
    UniGeneiMfa.8229.

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB125168 mRNA. Translation: BAD51956.1 .
    UniGenei Mfa.8229.

    3D structure databases

    ProteinModelPortali Q60HF9.
    SMRi Q60HF9. Positions 49-510.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q60HF9.

    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. "Isolation and characterization of cDNA for macaque neurological disease genes."
      Kusuda J., Osada N., Tanuma R., Hirata M., Sugano S., Hashimoto K.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Occipital cortex.

    Entry informationi

    Entry nameiFUMH_MACFA
    AccessioniPrimary (citable) accession number: Q60HF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 12, 2005
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 60 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

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3