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Q0VC74

- TMLH_BOVIN

UniProt

Q0VC74 - TMLH_BOVIN

Protein

Trimethyllysine dioxygenase, mitochondrial

Gene

TMLHE

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (05 Sep 2006)
      Previous versions | rss
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    Functioni

    Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).By similarity

    Catalytic activityi

    N6,N6,N(6)-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N(6)-trimethyl-L-lysine + succinate + CO2.

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity
    Ascorbate.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi242 – 2421Iron; catalyticBy similarity
    Metal bindingi244 – 2441Iron; catalyticBy similarity
    Metal bindingi389 – 3891Iron; catalyticBy similarity

    GO - Molecular functioni

    1. iron ion binding Source: InterPro
    2. L-ascorbic acid binding Source: InterPro
    3. oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Source: Ensembl
    4. trimethyllysine dioxygenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. carnitine biosynthetic process Source: UniProtKB-UniPathway
    2. negative regulation of oxidoreductase activity Source: Ensembl

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Carnitine biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_227979. Carnitine synthesis.
    UniPathwayiUPA00118.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Trimethyllysine dioxygenase, mitochondrial (EC:1.14.11.8)
    Alternative name(s):
    Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
    TML hydroxylase
    TML-alpha-ketoglutarate dioxygenase
    Short name:
    TML dioxygenase
    Short name:
    TMLD
    Gene namesi
    Name:TMLHE
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1515MitochondrionBy similarityAdd
    BLAST
    Chaini16 – 421406Trimethyllysine dioxygenase, mitochondrialPRO_0000260156Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei236 – 2361N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PRIDEiQ0VC74.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000048142.

    Structurei

    3D structure databases

    ProteinModelPortaliQ0VC74.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the gamma-BBH/TMLD family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG2175.
    HOGENOMiHOG000210004.
    HOVERGENiHBG035650.
    KOiK00474.

    Family and domain databases

    InterProiIPR010376. DUF971.
    IPR003819. Taurine_dOase.
    IPR012776. Trimethyllysine_dOase.
    [Graphical view]
    PfamiPF06155. DUF971. 1 hit.
    PF02668. TauD. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR02410. carnitine_TMLD. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q0VC74-1 [UniParc]FASTAAdd to Basket

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    MWCHRLSHLQ SRLQDLLRGR VTRWALQQSN FKSLFPLAIY WHHTASKSLN    50
    CVWQQHEDHF ELQYANNVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV 100
    DLCIQPQTIH LDETTLFFTW PDGHVTRYDL DWLMKNSYEG QKQKVIQPRI 150
    LWNAEIYQQA QVPAVDFQTF LETKEGLKNF LQNFLLYGIA FVENVPPTQK 200
    HTEKLAERIS LIRETIYGRM WFFTSDFSRG DTAYTKLALD RHTDTTYFQE 250
    PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE 300
    YIENVGECQN HMIGVGPVLN IYPWNKELYL IRYNNYDRAV INTVPYDVVH 350
    RWYTAHRTLT RELRRPENEF WVKLKPGKVL FIDNWRVLHG RESFTGYRQL 400
    CGCYLTRDDV LNTARLLGLQ A 421
    Length:421
    Mass (Da):49,837
    Last modified:September 5, 2006 - v1
    Checksum:i6FADE146279CA760
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC120318 mRNA. Translation: AAI20319.1.
    RefSeqiNP_001069532.1. NM_001076064.1.
    UniGeneiBt.21098.

    Genome annotation databases

    GeneIDi535630.
    KEGGibta:535630.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC120318 mRNA. Translation: AAI20319.1 .
    RefSeqi NP_001069532.1. NM_001076064.1.
    UniGenei Bt.21098.

    3D structure databases

    ProteinModelPortali Q0VC74.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000048142.

    Proteomic databases

    PRIDEi Q0VC74.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 535630.
    KEGGi bta:535630.

    Organism-specific databases

    CTDi 55217.

    Phylogenomic databases

    eggNOGi COG2175.
    HOGENOMi HOG000210004.
    HOVERGENi HBG035650.
    KOi K00474.

    Enzyme and pathway databases

    UniPathwayi UPA00118 .
    Reactomei REACT_227979. Carnitine synthesis.

    Miscellaneous databases

    NextBioi 20876796.

    Family and domain databases

    InterProi IPR010376. DUF971.
    IPR003819. Taurine_dOase.
    IPR012776. Trimethyllysine_dOase.
    [Graphical view ]
    Pfami PF06155. DUF971. 1 hit.
    PF02668. TauD. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR02410. carnitine_TMLD. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Ascending colon.

    Entry informationi

    Entry nameiTMLH_BOVIN
    AccessioniPrimary (citable) accession number: Q0VC74
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: September 5, 2006
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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