Reviewed,
UniProtKB/Swiss-Prot Q92I02 (TRXB_RICCN)
Last modified
February 9, 2010.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thioredoxin reductase Short name=TRXR EC=1.8.1.9 | ||||
| Gene names |
| ||||
| Organism | Rickettsia conorii [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 781 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group |
Protein attributes
| Sequence length | 310 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | Thioredoxin + NADP+ = thioredoxin disulfide + NADPH. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | The active site is a redox-active disulfide bond. |
| Sequence similarities | Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW removal of superoxide radicalsInferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 310 | 310 | Thioredoxin reductase | PRO_0000166742 | |||||||
Regions | |||||||||||
| Nucleotide binding | 34 – 41 | 8 | FAD By similarity | ||||||||
| Nucleotide binding | 281 – 290 | 10 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 135 ↔ 138 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE006914 Genomic DNA. Translation: AAL03156.1. |
| PIR | B97777. |
| RefSeq | NP_360255.1. |
3D structure databases | |
| SMR | Q92I02. Positions 4-310. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 927711. |
| GenomeReviews | Gene locus RC0618 in contig AE006914_GR. |
| KEGG | rco:RC0618. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | CAICDGH. |
Enzyme and pathway databases | |
| BioCyc | RCON272944:RC0618-MONOMER. |
| BRENDA | 1.8.1.9. 267518. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR001327. Pyr_OxRdtase_NAD_bd. 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 | TRXB_RICCN | ||||||||
| Accession | Primary (citable) accession number: Q92I02 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Rickettsia conorii (strain Malish 7): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


