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P14408

- FUMH_RAT

UniProt

P14408 - FUMH_RAT

Protein

Fumarate hydratase, mitochondrial

Gene

Fh

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    (S)-malate = fumarate + H2O.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei144 – 1441SubstrateBy similarity

    GO - Molecular functioni

    1. fumarate hydratase activity Source: RGD

    GO - Biological processi

    1. fumarate metabolic process Source: RGD
    2. malate metabolic process Source: RGD
    3. tricarboxylic acid cycle Source: RGD

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Tricarboxylic acid cycle

    Enzyme and pathway databases

    SABIO-RKP14408.
    UniPathwayiUPA00223; UER01007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fumarate hydratase, mitochondrial (EC:4.2.1.2)
    Short name:
    Fumarase
    Gene namesi
    Name:Fh
    Synonyms:Fh1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2614. Fh.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: RGD
    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 – 4141MitochondrionAdd
    BLAST
    Chaini42 – 507466Fumarate hydratase, mitochondrialPRO_0000010325Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei58 – 581N6-acetyllysine; alternateBy similarity
    Modified residuei58 – 581N6-succinyllysine; alternateBy similarity
    Modified residuei63 – 631N6-acetyllysine; alternateBy similarity
    Modified residuei63 – 631N6-succinyllysine; alternateBy similarity
    Modified residuei77 – 771N6-acetyllysine; alternateBy similarity
    Modified residuei77 – 771N6-succinyllysine; alternateBy similarity
    Modified residuei91 – 911N6-acetyllysineBy similarity
    Modified residuei112 – 1121N6-acetyllysine; alternateBy similarity
    Modified residuei112 – 1121N6-succinyllysine; alternateBy similarity
    Modified residuei119 – 1191N6-acetyllysine; alternateBy similarity
    Modified residuei119 – 1191N6-succinyllysine; alternateBy similarity
    Modified residuei210 – 2101N6-acetyllysineBy similarity
    Modified residuei220 – 2201N6-acetyllysine; alternateBy similarity
    Modified residuei220 – 2201N6-succinyllysine; alternateBy similarity
    Modified residuei289 – 2891N6-acetyllysine; alternateBy similarity
    Modified residuei289 – 2891N6-succinyllysine; alternateBy similarity
    Modified residuei464 – 4641N6-succinyllysineBy similarity
    Modified residuei470 – 4701N6-succinyllysineBy similarity
    Modified residuei499 – 4991N6-acetyllysineBy similarity

    Post-translational modificationi

    Isoform Cytoplasmic is acetylated at position 2.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP14408.
    PRIDEiP14408.

    PTM databases

    PhosphoSiteiP14408.

    Expressioni

    Gene expression databases

    GenevestigatoriP14408.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    IntActiP14408. 1 interaction.
    STRINGi10116.ENSRNOP00000004917.

    Structurei

    3D structure databases

    ProteinModelPortaliP14408.
    SMRiP14408. Positions 46-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni173 – 1764B siteBy similarity
    Regioni183 – 1853Substrate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0114.
    HOGENOMiHOG000061736.
    HOVERGENiHBG002183.
    InParanoidiP14408.
    PhylomeDBiP14408.

    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: P14408-1) [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

    MNRAFCLLAR SRRFPRVPSA GAVLSGEAAT LPRCAPNVVR MASQNSFRIE    50
    YDTFGELKVP TDKYYGAQTV RSTMNFKIGG ATERMPIPVI KAFGILKRAA 100
    AEVNQEYGLD PKIASAIMKA ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV 150
    NEVISNRAIE MLGGELGSKK PVHPNDHVNK SQSSNDTFPT AMHIAAALEV 200
    HQVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT LGQEFSGYVQ 250
    QVQYAMERIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL 300
    PFVTAPNKFE ALAAHDALVE LSGAMNTTAC SLMKIANDIR FLGSGPRSGL 350
    GELILPENEP GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF 400
    ELNVFKPMMI KNVLHSARLL GDASVSFTEN CVVGIQANTE RINKLMNESL 450
    MLVTALNPHI GYDKAAKIAK TAHKNGSTLK KTAIELGYLT AEQFDEWVKP 500
    KDMLGPK 507
    Length:507
    Mass (Da):54,464
    Last modified:January 1, 1990 - v1
    Checksum:i0304255E04C0D7D8
    GO
    Isoform Cytoplasmic (identifier: P14408-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-40: Missing.

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

    Show »
    Length:467
    Mass (Da):50,170
    Checksum:i33CC61C8CC024663
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4040Missing in isoform Cytoplasmic. CuratedVSP_018968Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04473 mRNA. Translation: AAA41177.1.
    PIRiA31424. UFRT.
    UniGeneiRn.29782.

    Genome annotation databases

    UCSCiRGD:2614. rat. [P14408-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04473 mRNA. Translation: AAA41177.1 .
    PIRi A31424. UFRT.
    UniGenei Rn.29782.

    3D structure databases

    ProteinModelPortali P14408.
    SMRi P14408. Positions 46-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P14408. 1 interaction.
    STRINGi 10116.ENSRNOP00000004917.

    PTM databases

    PhosphoSitei P14408.

    Proteomic databases

    PaxDbi P14408.
    PRIDEi P14408.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:2614. rat. [P14408-1 ]

    Organism-specific databases

    RGDi 2614. Fh.

    Phylogenomic databases

    eggNOGi COG0114.
    HOGENOMi HOG000061736.
    HOVERGENi HBG002183.
    InParanoidi P14408.
    PhylomeDBi P14408.

    Enzyme and pathway databases

    UniPathwayi UPA00223 ; UER01007 .
    SABIO-RK P14408.

    Miscellaneous databases

    PROi P14408.

    Gene expression databases

    Genevestigatori P14408.

    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. "Rat liver mitochondrial and cytosolic fumarases with identical amino acid sequences are encoded from a single gene."
      Suzuki T., Sato M., Yoshida T., Tuboi S.
      J. Biol. Chem. 264:2581-2586(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
      Tissue: Liver.
    2. Lubec G., Afjehi-Sadat L., Chen W.-Q.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 266-283 AND 420-441, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Hippocampus and Spinal cord.

    Entry informationi

    Entry nameiFUMH_RAT
    AccessioniPrimary (citable) accession number: P14408
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 133 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