Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q0VC74 (TMLH_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:TMLHE
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML) By similarity.

Catalytic activity

N6,N6,N(6)-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N(6)-trimethyl-L-lysine + succinate + CO2.

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Ascorbate By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1515Mitochondrion By similarity
Chain16 – 421406Trimethyllysine dioxygenase, mitochondrial
PRO_0000260156

Sites

Metal binding2421Iron; catalytic By similarity
Metal binding2441Iron; catalytic By similarity
Metal binding3891Iron; catalytic By similarity

Amino acid modifications

Modified residue2361N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0VC74 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 6FADE146279CA760

FASTA42149,837
        10         20         30         40         50         60 
MWCHRLSHLQ SRLQDLLRGR VTRWALQQSN FKSLFPLAIY WHHTASKSLN CVWQQHEDHF 

        70         80         90        100        110        120 
ELQYANNVMR FDYVWLRDHC RSASCYNSKT HQRSLDTASV DLCIQPQTIH LDETTLFFTW 

       130        140        150        160        170        180 
PDGHVTRYDL DWLMKNSYEG QKQKVIQPRI LWNAEIYQQA QVPAVDFQTF LETKEGLKNF 

       190        200        210        220        230        240 
LQNFLLYGIA FVENVPPTQK HTEKLAERIS LIRETIYGRM WFFTSDFSRG DTAYTKLALD 

       250        260        270        280        290        300 
RHTDTTYFQE PCGIQVFHCL KHEGTGGRTL LVDGFYAAEQ VLQKAPEEFE LLSKVPLKHE 

       310        320        330        340        350        360 
YIENVGECQN HMIGVGPVLN IYPWNKELYL IRYNNYDRAV INTVPYDVVH RWYTAHRTLT 

       370        380        390        400        410        420 
RELRRPENEF WVKLKPGKVL FIDNWRVLHG RESFTGYRQL CGCYLTRDDV LNTARLLGLQ 


A 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC120318 mRNA. Translation: AAI20319.1.
RefSeqNP_001069532.1. NM_001076064.1.
UniGeneBt.21098.

3D structure databases

ProteinModelPortalQ0VC74.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000048142.

Proteomic databases

PRIDEQ0VC74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID535630.
KEGGbta:535630.

Organism-specific databases

CTD55217.

Phylogenomic databases

eggNOGCOG2175.
HOGENOMHOG000210004.
HOVERGENHBG035650.
KOK00474.

Enzyme and pathway databases

UniPathwayUPA00118.

Family and domain databases

InterProIPR010376. DUF971.
IPR003819. Taurine_dOase.
IPR012776. Trimethyllysine_dOase.
[Graphical view]
PANTHERPTHR10696:SF2. PTHR10696:SF2. 1 hit.
PfamPF06155. DUF971. 1 hit.
PF02668. TauD. 1 hit.
[Graphical view]
TIGRFAMsTIGR02410. carnitine_TMLD. 1 hit.
ProtoNetSearch...

Other

NextBio20876796.

Entry information

Entry nameTMLH_BOVIN
AccessionPrimary (citable) accession number: Q0VC74
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: September 5, 2006
Last modified: April 16, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways