Q81PQ0 (T23O_BACAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
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: Tryptophan 2,3-dioxygenase Short name=TDO EC=1.13.11.11 Alternative name(s): Tryptamin 2,3-dioxygenase Tryptophan oxygenase Short name=TO Short name=TRPO Tryptophan pyrrolase Tryptophanase | ||||
| Gene names |
| ||||
| Organism | Bacillus anthracis | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 279 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the oxidative cleavage of the L-tryptophan (L-Trp) pyrrole ring By similarity. |
| Catalytic activity | L-tryptophan + O2 = N-formyl-L-kynurenine. |
| Cofactor | Binds 2 heme groups per tetramer By similarity. |
| Pathway | |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the tryptophan 2,3-dioxygenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tryptophan catabolism |
| Ligand | Heme Iron Metal-binding |
| Molecular function | Dioxygenase Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | protein homotetramerization Inferred from sequence or structural similarity. Source: UniProtKB tryptophan catabolic process to kynurenineInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | heme binding Inferred from sequence or structural similarity. Source: UniProtKB tryptophan 2,3-dioxygenase activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 279 | 279 | Tryptophan 2,3-dioxygenase | PRO_0000360084 | |||||
Regions | |||||||||
| Region | 23 – 27 | 5 | Substrate binding By similarity | ||||||
| Region | 48 – 52 | 5 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 237 | 1 | Iron (heme axial ligand) By similarity | ||||||
| Binding site | 110 | 1 | Substrate By similarity | ||||||
| Binding site | 114 | 1 | Substrate By similarity | ||||||
| Binding site | 121 | 1 | Heme By similarity | ||||||
| Binding site | 251 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
| [3] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP26587.1. AE017334 Genomic DNA. Translation: AAT31867.1. AE017225 Genomic DNA. Translation: AAT54875.1. |
| RefSeq | NP_845101.1. NC_003997.3. YP_019392.1. NC_007530.2. YP_028824.1. NC_005945.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1YW0 based on UniProtKB Q8PDA8. |
| ProteinModelPortal | Q81PQ0. |
| SMR | Q81PQ0. Positions 20-279. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000008130; EBBACP00000007886; EBBACG00000008122. EBBACT00000016170; EBBACP00000015791; EBBACG00000016162. EBBACT00000021185; EBBACP00000020670; EBBACG00000021176. |
| GeneID | 1088379. 2819588. 2849155. |
| GenomeReviews | Gene locus BA_2751 in contig AE016879_GR. Gene locus BAS2565 in contig AE017225_GR. Gene locus GBAA_2751 in contig AE017334_GR. |
| KEGG | ban:BA_2751. bar:GBAA_2751. bat:BAS2565. |
| TIGR | BA_2751. GBAA_2751. |
Phylogenomic databases | |
| GeneTree | EBGT00050000004238. |
| HOGENOM | HBG647485. |
| OMA | KLLVDQV. |
| ProtClustDB | CLSK904616. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS2565-MONOMER. BANT261594:GBAA2751-MONOMER. |
Family and domain databases | |
| InterPro | IPR017485. Trp_2-3-dOase_bac. IPR004981. Trp_2_3_dOase. [Graphical view] |
| KO | K00453. |
| PANTHER | PTHR10138. Trp_2_3_dOase. 1 hit. |
| Pfam | PF03301. Trp_dioxygenase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03036. Trp_2_3_diox. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | T23O_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81PQ0 Secondary accession number(s): Q6HXW4, Q6KRY6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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