Reviewed,
UniProtKB/Swiss-Prot Q96UB1 (TMLH_NEUCR)
Last modified
June 16, 2009.
Version 47.
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 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 |
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| Organism | Neurospora crassa [Complete proteome] | ||||
| Taxonomic identifier | 5141 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora |
Protein attributes
| Sequence length | 471 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Converts trimethyllysine (TML) into hydroxytrimethyllysine (HTML). |
| Catalytic activity | N6,N6,N(6)-trimethyl-L-lysine + 2-oxoglutarate + O2 = 3-hydroxy-N6,N6,N(6)-trimethyl-L-lysine + succinate + CO2. |
| Cofactor | Iron. Ascorbate. |
| Pathway | |
| Subcellular location | Cytoplasm Probable. |
| Sequence similarities | Belongs to the gamma-BBH/TMLD family. |
| Sequence caution | The sequence CAD11356.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence EAA31955.2 differs from that shown. Reason: Erroneous gene model prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carnitine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Iron |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carnitine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm 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: UniProtKB-KW 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)
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| AJ421151 mRNA. Translation: CAD12887.1. AL451018 Genomic DNA. Translation: CAD11356.1. Sequence problems. AABX02000011 Genomic DNA. Translation: EAA31955.2. Sequence problems. | |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.14.11.8. 266. |
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_NEUCR | ||||||||
| Accession | Primary (citable) accession number: Q96UB1 Secondary accession number(s): Q7S7S2, Q8NIQ9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


