Reviewed, UniProtKB/Swiss-Prot Q91ZE0 (TMLH_MOUSE)

Names and origin

Protein names

Recommended name:
    Trimethyllysine dioxygenase, mitochondrial
    EC=1.14.11.8
Alternative name(s):
    Epsilon-trimethyllysine 2-oxoglutarate dioxygenase
    TML-alpha-ketoglutarate dioxygenase
      Short name=TML dioxygenase
      Short name=TMLD
    TML hydroxylase

Gene names

Name:	Tmlhe
Synonyms:	Tmlh

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML).
Catalytic activity	N6,N6,N(6)-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N(6)-trimethyl-L-lysine + succinate + CO2.
Cofactor	Iron. Ascorbate.
Pathway	Amine and polyamine biosynthesis; carnitine biosynthesis.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the gamma-BBH/TMLD family.

Ontologies

Keywords
Biological process	Carnitine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	Iron
Molecular function	Dioxygenase Oxidoreductase
Gene Ontology (GO)
Biological process	carnitine biosynthetic process Inferred from direct assay. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-ascorbic acid binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from direct assay. Source: MGI trimethyllysine dioxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – ?		Mitochondrion Potential
	Chain	? – 421		Trimethyllysine dioxygenase, mitochondrial		PRO_0000002796

Sequences

	Sequence		Length	Mass (Da)
	Q91ZE0-1 [UniParc]. Last modified June 20, 2002. Version 2. Checksum: 1474AD5742E88F43	FASTA	421	49,610
	10 20 30 40 50 60 MWYHKLLHQQ SRLRNLMKRG NIAQGLHLSN FKSLFSSSIH WCHTTSKSVN CTWHQHEDHL 70 80 90 100 110 120 ELQYAGTVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIKPKTVH LDETMLFFTW 130 140 150 160 170 180 PDGHVTRYDL DWLVKNSYEG QKQKVIQPRI LWNSKLYQQA QVPSVDFQCF LETNEGLKKF 190 200 210 220 230 240 LQNFLLYGIA FVENVPPTEE HTEKLAERIS LIRETIYGRM WYFTSDFSRG DTAYTKLALD 250 260 270 280 290 300 RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAQQ VLQKAPEEFE LLSKVPLKHE 310 320 330 340 350 360 YIENVGQCHN HMIGVGPILN IYPWNKELYL IRYNNYDRAV INTVPYDVVH RWYTAHRTLT 370 380 390 400 410 420 TELRRPENEL WVKLKPGKVL FIDNWRVLHG RESFTGYRQL CGCYLTRDDV LNTARLLGLH A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular and biochemical characterization of rat epsilon-N-trimethyllysine hydroxylase, the first enzyme of carnitine biosynthesis." Vaz F.M., Ofman R., Westinga K., Back J.W., Wanders R.J.A. J. Biol. Chem. 276:33512-33517(2001) [PubMed: 11431483] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-421. Strain: FVB/N.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY033513 mRNA. Translation: AAK54387.1. Different initiation. BC010495 mRNA. Translation: AAH10495.1.
IPI	IPI00129163.
RefSeq	NP_620097.1.
UniGene	Mm.394228
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q91ZE0.
Genome annotation databases
Ensembl	ENSMUSG00000079834. Mus musculus. [Contig view]
GeneID	192289.
KEGG	mmu:192289.
Organism-specific databases
MGI	MGI:2180203. Tmlhe.
Phylogenomic databases
HOVERGEN	Q91ZE0.
OMA	Q91ZE0. HEDHLEL.
Enzyme and pathway databases
BRENDA	1.14.11.8. 244.
Gene expression databases
ArrayExpress	Q91ZE0.
Bgee	Q91ZE0.
CleanEx	MM_TMLHE.
Family and domain databases
InterPro	IPR003819. Taurine_dOase. IPR012776. Trimethyllysine_dOase. [Graphical view]
PANTHER	PTHR10696:SF2. tMLys_dOase. 1 hit.
Pfam	PF02668. TauD. 1 hit. [Graphical view]
TIGRFAMs	TIGR02410. carnitine_TMLD. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	371290.
SOURCE	Search...

Entry information

Entry name

TMLH_MOUSE

Accession

Primary (citable) accession number: Q91ZE0
Secondary accession number(s): Q91XH1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2002
Last sequence update:	June 20, 2002
Last modified:	June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)