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   16-JUN-2009, entry version 27.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
CC       hydroxytrimethyllysine (HTML) (By similarity).
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 (By similarity).
CC   -!- COFACTOR: Ascorbate (By similarity).
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; BC120318; AAI20319.1; -; mRNA.
DR   IPI; IPI00721209; -.
DR   RefSeq; NP_001069532.1; -.
DR   UniGene; Bt.21098; -.
DR   Ensembl; ENSBTAG00000011648; Bos taurus.
DR   GeneID; 535630; -.
DR   KEGG; bta:535630; -.
DR   HOVERGEN; Q0VC74; -.
DR   BRENDA; 1.14.11.8; 251.
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...; IEA:UniProtKB-KW.
DR   GO; GO:0050353; F:trimethyllysine dioxygenase activity; IEA:EC.
DR   GO; GO:0045329; P:carnitine biosynthetic process; IEA:UniProtKB-KW.
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_0000260156.
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
//