Q5F4B3 (TMLH_CHICK) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 51.
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 | Gallus gallus (Chicken) | ||||
| Taxonomic identifier | 9031 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus |
Protein attributes
| Sequence length | 418 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 | |
| Sequence similarities | Belongs to the gamma-BBH/TMLD family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carnitine biosynthesis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | carnitine biosynthetic process 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 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: 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 | ? – 418 | Trimethyllysine dioxygenase, mitochondrial | PRO_0000260157 | ||||||
Sites | |||||||||
| Metal binding | 239 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 241 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 386 | 1 | Iron; catalytic By similarity | ||||||
Sequences
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References
| [1] | "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis." Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M. Genome Biol. 6:R6.1-R6.9(2005) [PubMed: 15642098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: CB. Tissue: Bursa of Fabricius. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ851387 mRNA. Translation: CAH65021.1. |
| IPI | IPI00598008. |
| RefSeq | NP_001012593.1. NM_001012575.1. |
| UniGene | Gga.18010. |
3D structure databases | |
| ProteinModelPortal | Q5F4B3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSGALT00000012043; ENSGALP00000012029; ENSGALG00000007443. |
| GeneID | 422296. |
| KEGG | gga:422296. |
Organism-specific databases | |
| CTD | 55217. |
Phylogenomic databases | |
| eggNOG | veNOG13035. |
| GeneTree | ENSGT00530000063582. |
| HOGENOM | HBG445343. |
| HOVERGEN | HBG035650. |
| InParanoid | Q5F4B3. |
| OMA | LCGCYLT. |
| OrthoDB | EOG4QRH4C. |
| PhylomeDB | Q5F4B3. |
Family and domain databases | |
| InterPro | IPR010376. DUF971. IPR003819. Taurine_dOase. IPR012776. Trimethyllysine_dOase. [Graphical view] |
| KO | K00474. |
| Pfam | PF06155. DUF971. 1 hit. PF02668. TauD. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR02410. Carnitine_TMLD. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | TMLH_CHICK | ||||||||
| Accession | Primary (citable) accession number: Q5F4B3 | ||||||||
| 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