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Protein

Trimethyllysine dioxygenase, mitochondrial

Gene

TMLHE

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

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

Protein has several cofactor binding sites:
  • Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity
  • L-ascorbateBy 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
Complete GO annotation...

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
Complete GO annotation...

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.

Expressioni

Gene expression databases

ExpressionAtlasiQ0VC74. baseline.

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.
InParanoidiQ0VC74.
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

« Hide

        10         20         30         40         50
MWCHRLSHLQ SRLQDLLRGR VTRWALQQSN FKSLFPLAIY WHHTASKSLN
60 70 80 90 100
CVWQQHEDHF ELQYANNVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV
110 120 130 140 150
DLCIQPQTIH LDETTLFFTW PDGHVTRYDL DWLMKNSYEG QKQKVIQPRI
160 170 180 190 200
LWNAEIYQQA QVPAVDFQTF LETKEGLKNF LQNFLLYGIA FVENVPPTQK
210 220 230 240 250
HTEKLAERIS LIRETIYGRM WFFTSDFSRG DTAYTKLALD RHTDTTYFQE
260 270 280 290 300
PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE
310 320 330 340 350
YIENVGECQN HMIGVGPVLN IYPWNKELYL IRYNNYDRAV INTVPYDVVH
360 370 380 390 400
RWYTAHRTLT RELRRPENEF WVKLKPGKVL FIDNWRVLHG RESFTGYRQL
410 420
CGCYLTRDDV LNTARLLGLQ A
Length:421
Mass (Da):49,837
Last modified:September 5, 2006 - v1
Checksum:i6FADE146279CA760
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
BC120318 mRNA. Translation: AAI20319.1.
RefSeqiNP_001069532.1. NM_001076064.1.
UniGeneiBt.21098.

3D structure databases

ProteinModelPortaliQ0VC74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000048142.

Proteomic databases

PRIDEiQ0VC74.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi535630.
KEGGibta:535630.

Organism-specific databases

CTDi55217.

Phylogenomic databases

eggNOGiCOG2175.
HOGENOMiHOG000210004.
HOVERGENiHBG035650.
InParanoidiQ0VC74.
KOiK00474.

Enzyme and pathway databases

UniPathwayiUPA00118.
ReactomeiREACT_227979. Carnitine synthesis.

Miscellaneous databases

NextBioi20876796.

Gene expression databases

ExpressionAtlasiQ0VC74. baseline.

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.
ProtoNetiSearch...

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: March 4, 2015
This is version 70 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.