Reviewed,
UniProtKB/Swiss-Prot Q0VC74 (TMLH_BOVIN)
Last modified
November 25, 2008.
Version 23.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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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 |
| ||
| Organism | Bos taurus (Bovine) | ||
| 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 | N(6),N(6),N(6)-trimethyl-L-lysine + 2-oxoglutarate + O(2) = 3-hydroxy-N(6),N(6),N(6)-trimethyl-L-lysine + succinate + CO(2). |
| Cofactor | Iron By similarity. Ascorbate By similarity. |
| Pathway | |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Mitochondrion matrixBy 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 electronic annotation. Source: InterPro oxidation reductionInferred 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 activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred from electronic annotation. Source: UniProtKB-KW trimethyllysine dioxygenase activityInferred from electronic annotation. Source: InterPro |
| 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_0000260156 | |||
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 | |
|---|---|
| BC120318 mRNA. Translation: AAI20319.1. | |
| RefSeq | NP_001069532.1. |
| UniGene | Bt.21098 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAG00000011648. Bos taurus. [Contig view] |
| GeneID | 535630. |
| KEGG | bta:535630. |
Phylogenomic databases | |
| HOVERGEN | Q0VC74. |
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... |
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 project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


