Q0VC74 (TMLH_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 59.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
| ||
| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
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) 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 | |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the gamma-BBH/TMLD family. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 15 | 15 | Mitochondrion By similarity | ||||||
| Chain | 16 – 421 | 406 | Trimethyllysine dioxygenase, mitochondrial | PRO_0000260156 | |||||
Sites | |||||||||
| Metal binding | 242 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 244 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 389 | 1 | Iron; catalytic By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 236 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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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. |
| IPI | IPI00906767. |
| RefSeq | NP_001069532.1. NM_001076064.1. |
| UniGene | Bt.21098. |
3D structure databases | |
| ProteinModelPortal | Q0VC74. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9913.ENSBTAP00000048142. |
Proteomic databases | |
| PRIDE | Q0VC74. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 535630. |
| KEGG | bta:535630. |
Organism-specific databases | |
| CTD | 55217. |
Phylogenomic databases | |
| eggNOG | COG2175. |
| HOGENOM | HOG000210004. |
| HOVERGEN | HBG035650. |
| KO | K00474. |
Enzyme and pathway databases | |
| BioCyc | CATTLE:535630-MONOMER. |
| UniPathway | UPA00118. |
Gene expression databases | |
| ArrayExpress | Q0VC74. |
Family and domain databases | |
| InterPro | IPR010376. DUF971. IPR003819. Taurine_dOase. IPR012776. Trimethyllysine_dOase. [Graphical view] |
| PANTHER | PTHR10696:SF2. PTHR10696:SF2. 1 hit. |
| Pfam | PF06155. DUF971. 1 hit. PF02668. TauD. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02410. carnitine_TMLD. 1 hit. |
| ProtoNet | Search... |
Other | |
| NextBio | 20876796. |
Entry information
| Entry name | TMLH_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q0VC74 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
