D5TE22 (D5TE22_LEGP2) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 16.
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 |
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| Organism | Legionella pneumophila serogroup 1 (strain 2300/99 Alcoy) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 423212 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella › ![]() |
Protein attributes
| Sequence length | 316 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 SAAS SAAS000103 RuleBase RU003880 Flavoprotein RuleBase RU003880 SAAS SAAS000103 NADP RuleBase RU003881 |
| Molecular function | Oxidoreductase RuleBase RU003880 SAAS SAAS000103 EMBL ADG25106.1 |
| 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
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References
| [1] | "Legionella pneumophila pangenome reveals strain-specific virulence factors." D'Auria G., Jimenez-Hernandez N., Peris-Bondia F., Moya A., Latorre A. BMC Genomics 11:181-181(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 2300/99 Alcoy EMBL ADG25106.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001828 Genomic DNA. Translation: ADG25106.1. |
| RefSeq | YP_003619058.1. NC_014125.1. |
3D structure databases | |
| ProteinModelPortal | D5TE22. |
| SMR | D5TE22. Positions 4-316. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADG25106; ADG25106; lpa_02558. |
| GeneID | 9129641. |
| KEGG | lpa:lpa_02558. |
| PATRIC | 38181701. VBILegPne70474_1959. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000072912. |
| KO | K00384. |
Enzyme and pathway databases | |
| BioCyc | LPNE423212:GHRR-1887-MONOMER. |
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] |
| 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 | D5TE22_LEGP2 | ||||||||
| Accession | Primary (citable) accession number: D5TE22 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
