ID   TMLH_MOUSE              Reviewed;         421 AA.
AC   Q91ZE0; Q91XH1;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 2.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Trimethyllysine dioxygenase, mitochondrial;
DE            EC=1.14.11.8;
DE   AltName: Full=Epsilon-trimethyllysine 2-oxoglutarate dioxygenase;
DE   AltName: Full=TML-alpha-ketoglutarate dioxygenase;
DE            Short=TML dioxygenase;
DE            Short=TMLD;
DE   AltName: Full=TML hydroxylase;
DE   Flags: Precursor;
GN   Name=Tmlhe; Synonyms=Tmlh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-421.
RC   STRAIN=FVB/N;
RX   MEDLINE=21423953; PubMed=11431483; DOI=10.1074/jbc.M105929200;
RA   Vaz F.M., Ofman R., Westinga K., Back J.W., Wanders R.J.A.;
RT   "Molecular and biochemical characterization of rat epsilon-N-
RT   trimethyllysine hydroxylase, the first enzyme of carnitine
RT   biosynthesis.";
RL   J. Biol. Chem. 276:33512-33517(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Converts trimethyllysine (TML) into
CC       hydroxytrimethyllysine (HTML).
CC   -!- CATALYTIC ACTIVITY: N(6),N(6),N(6)-trimethyl-L-lysine + 2-
CC       oxoglutarate + O(2) = 3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine
CC       + succinate + CO(2).
CC   -!- COFACTOR: Iron.
CC   -!- COFACTOR: Ascorbate.
CC   -!- PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the gamma-BBH/TMLD family.
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DR   EMBL; AY033513; AAK54387.1; ALT_INIT; mRNA.
DR   EMBL; BC010495; AAH10495.1; -; mRNA.
DR   IPI; IPI00129163; -.
DR   RefSeq; NP_620097.1; -.
DR   UniGene; Mm.394228; -.
DR   PRIDE; Q91ZE0; -.
DR   Ensembl; ENSMUSG00000079834; Mus musculus.
DR   GeneID; 192289; -.
DR   KEGG; mmu:192289; -.
DR   MGI; MGI:2180203; Tmlhe.
DR   HOVERGEN; Q91ZE0; -.
DR   OMA; Q91ZE0; HEDHLEL.
DR   BRENDA; 1.14.11.8; 244.
DR   NextBio; 371290; -.
DR   ArrayExpress; Q91ZE0; -.
DR   Bgee; Q91ZE0; -.
DR   CleanEx; MM_TMLHE; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IDA:MGI.
DR   GO; GO:0050353; F:trimethyllysine dioxygenase activity; IEA:EC.
DR   GO; GO:0045329; P:carnitine biosynthetic process; IDA:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003819; Taurine_dOase.
DR   InterPro; IPR012776; Trimethyllysine_dOase.
DR   PANTHER; PTHR10696:SF2; tMLys_dOase; 1.
DR   Pfam; PF02668; TauD; 1.
DR   TIGRFAMs; TIGR02410; carnitine_TMLD; 1.
PE   2: Evidence at transcript level;
KW   Carnitine biosynthesis; Dioxygenase; Iron; Mitochondrion;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    421       Trimethyllysine dioxygenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000002796.
SQ   SEQUENCE   421 AA;  49610 MW;  1474AD5742E88F43 CRC64;
     MWYHKLLHQQ SRLRNLMKRG NIAQGLHLSN FKSLFSSSIH WCHTTSKSVN CTWHQHEDHL
     ELQYAGTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTVH LDETMLFFTW
     PDGHVTRYDL DWLVKNSYEG QKQKVIQPRI LWNSKLYQQA QVPSVDFQCF LETNEGLKKF
     LQNFLLYGIA FVENVPPTEE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD
     RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAQQ VLQKAPEEFE LLSKVPLKHE
     YIENVGQCHN HMIGVGPILN IYPWNKELYL IRYNNYDRAV INTVPYDVVH RWYTAHRTLT
     TELRRPENEL WVKLKPGKVL FIDNWRVLHG RESFTGYRQL CGCYLTRDDV LNTARLLGLH
     A
//