A0RKU5 (A0RKU5_BACAH) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 41.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Thioredoxin reductase RuleBase RU003881 EC=1.8.1.9 RuleBase RU003881 | ||||
| Gene names |
| ||||
| Organism | Bacillus thuringiensis (strain Al Hakam) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 412694 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 321 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | Thioredoxin + NADP+ = thioredoxin disulfide + NADPH. RuleBase RU003881 |
| Cofactor | Binds 1 FAD per subunit By similarity. RuleBase RU003881 |
| Sequence similarities | Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. RuleBase RU003880 |
Ontologies
| Keywords | |
|---|---|
| Domain | Redox-active center RuleBase RU003880 |
| Ligand | FAD RuleBase RU003880 Flavoprotein RuleBase RU003880 |
| Molecular function | Oxidoreductase RuleBase RU003880 EMBL ABK87838.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | removal of superoxide radicals Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequences
| ||||||||||||||||||
References
| [1] | "The complete genome sequence of Bacillus thuringiensis Al Hakam." Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Green L.D., Han C.S. Brettin T.S.J. Bacteriol. 189:3680-3681(2007) [PubMed: 17337577] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000485 Genomic DNA. Translation: ABK87838.1. |
| RefSeq | YP_897345.1. NC_008600.1. |
3D structure databases | |
| ProteinModelPortal | A0RKU5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A0RKU5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000066595; EBBACP00000064832; EBBACG00000066586. |
| GeneID | 4542898. |
| GenomeReviews | Gene locus BALH_4650 in contig CP000485_GR. |
| KEGG | btl:BALH_4650. |
| PATRIC | 19002390. VBIBacThu63319_5165. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0492. |
| GeneTree | EBGT00050000000432. |
| HOGENOM | HBG669726. |
| OMA | RMETKIP. |
| ProtClustDB | CLSK2758187. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR005982. Thioredox_Rdtase. [Graphical view] |
| KO | K00384. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00469. PNDRDTASEII. |
| TIGRFAMs | TIGR01292. TRX_reduct. 1 hit. |
| PROSITE | PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | A0RKU5_BACAH | ||||||||
| Accession | Primary (citable) accession number: A0RKU5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with