ID   TMLH_BOVIN              Reviewed;         421 AA.
AC   Q0VC74;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Trimethyllysine dioxygenase, mitochondrial;
DE            EC=1.14.11.8 {ECO:0000250|UniProtKB:Q9NVH6};
DE   AltName: Full=Epsilon-trimethyllysine 2-oxoglutarate dioxygenase;
DE   AltName: Full=TML hydroxylase;
DE   AltName: Full=TML-alpha-ketoglutarate dioxygenase;
DE            Short=TML dioxygenase;
DE            Short=TMLD;
DE   Flags: Precursor;
GN   Name=TMLHE;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts trimethyllysine (TML) into hydroxytrimethyllysine
CC       (HTML). {ECO:0000250|UniProtKB:Q9NVH6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysine + O2 =
CC         (3S)-3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + CO2 + succinate;
CC         Xref=Rhea:RHEA:14181, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58100,
CC         ChEBI:CHEBI:141499; EC=1.14.11.8;
CC         Evidence={ECO:0000250|UniProtKB:Q9NVH6};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q91ZW6}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q9NVH6}.
CC   -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family. {ECO:0000305}.
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DR   EMBL; BC120318; AAI20319.1; -; mRNA.
DR   RefSeq; NP_001069532.1; NM_001076064.1.
DR   AlphaFoldDB; Q0VC74; -.
DR   SMR; Q0VC74; -.
DR   STRING; 9913.ENSBTAP00000015469; -.
DR   PaxDb; Q0VC74; -.
DR   PRIDE; Q0VC74; -.
DR   Ensembl; ENSBTAT00000015469; ENSBTAP00000015469; ENSBTAG00000011648.
DR   GeneID; 535630; -.
DR   KEGG; bta:535630; -.
DR   CTD; 55217; -.
DR   VEuPathDB; HostDB:ENSBTAG00000011648; -.
DR   VGNC; VGNC:36134; TMLHE.
DR   eggNOG; KOG3889; Eukaryota.
DR   GeneTree; ENSGT00530000063582; -.
DR   HOGENOM; CLU_021859_2_0_1; -.
DR   InParanoid; Q0VC74; -.
DR   OMA; EEKVCIQ; -.
DR   OrthoDB; 868657at2759; -.
DR   UniPathway; UPA00118; -.
DR   Proteomes; UP000009136; Chromosome X.
DR   Bgee; ENSBTAG00000011648; Expressed in metanephros cortex and 104 other tissues.
DR   ExpressionAtlas; Q0VC74; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0050353; F:trimethyllysine dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0045329; P:carnitine biosynthetic process; ISS:UniProtKB.
DR   Gene3D; 3.30.2020.30; -; 1.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR010376; GBBH-like_N.
DR   InterPro; IPR038492; GBBH-like_N_sf.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   InterPro; IPR012776; Trimethyllysine_dOase.
DR   Pfam; PF06155; GBBH-like_N; 1.
DR   Pfam; PF02668; TauD; 1.
DR   TIGRFAMs; TIGR02410; carnitine_TMLD; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Carnitine biosynthesis; Dioxygenase; Iron; Metal-binding;
KW   Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide.
FT   TRANSIT         1..15
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           16..421
FT                   /note="Trimethyllysine dioxygenase, mitochondrial"
FT                   /id="PRO_0000260156"
FT   BINDING         242
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         244
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         389
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         236
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NVH6"
SQ   SEQUENCE   421 AA;  49837 MW;  6FADE146279CA760 CRC64;
     MWCHRLSHLQ SRLQDLLRGR VTRWALQQSN FKSLFPLAIY WHHTASKSLN CVWQQHEDHF
     ELQYANNVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIQPQTIH LDETTLFFTW
     PDGHVTRYDL DWLMKNSYEG QKQKVIQPRI LWNAEIYQQA QVPAVDFQTF LETKEGLKNF
     LQNFLLYGIA FVENVPPTQK HTEKLAERIS LIRETIYGRM WFFTSDFSRG DTAYTKLALD
     RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE
     YIENVGECQN HMIGVGPVLN IYPWNKELYL IRYNNYDRAV INTVPYDVVH RWYTAHRTLT
     RELRRPENEF WVKLKPGKVL FIDNWRVLHG RESFTGYRQL CGCYLTRDDV LNTARLLGLQ
     A