Reviewed,
UniProtKB/Swiss-Prot P39916 (TRXB_COXBU)
Last modified
November 24, 2009.
Version 76.
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 | Coxiella burnetii [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 777 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella |
Protein attributes
| Sequence length | 320 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 – 320 | 320 | Thioredoxin reductase | PRO_0000166728 | |||||||
Regions | |||||||||||
| Nucleotide binding | 36 – 43 | 8 | FAD By similarity | ||||||||
| Nucleotide binding | 287 – 296 | 10 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 136 ↔ 139 | Redox-active By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 21 | 1 | A → D in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 25 | 1 | A → V in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 51 | 1 | D → A in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 64 – 66 | 3 | QLM → KLL in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 74 – 77 | 4 | ERLD → GGALN in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 87 – 88 | 2 | EA → KP in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 92 | 1 | Q → P in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 98 | 1 | K → Q in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 127 | 1 | A → P in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 146 | 1 | G → A in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 158 | 1 | A → S in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 284 – 292 | 9 | AAGDVTDHV → PAVVVRGQL in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 296 – 298 | 3 | AIT → TIA in CAA53288. Ref.1 | ||||||||
| Sequence conflict | 306 | 1 | A → P in CAA53288. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Oswald W. Thesis (1994), Justus Liebig University / Frankfurt, Germany Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Nine Mile phase I / Bratislava. |
| [2] | "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. Heidelberg J.F.Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed: 12704232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Nine Mile phase I / RSA 493. |
Cross-references
Sequence databases | |
|---|---|
| X75627 Genomic DNA. Translation: CAA53288.1. AE016828 Genomic DNA. Translation: AAO90702.1. | |
| PIR | S43131. |
| RefSeq | NP_820188.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1209097. |
| GenomeReviews | Gene locus CBU_1193 in contig AE016828_GR. |
| KEGG | cbu:CBU_1193. |
| NMPDR | fig|227377.1.peg.1132. |
| TIGR | CBU_1193. |
Phylogenomic databases | |
| HOGENOM | P39916. |
| OMA | HCKLLIL |
Enzyme and pathway databases | |
| BioCyc | CBUR227377:CBU_1193-MON. |
| BRENDA | 1.8.1.9. 256353. |
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_COXBU | ||||||||
| Accession | Primary (citable) accession number: P39916 | ||||||||
| 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
| Coxiella burnetii Coxiella burnetii (strain RSA 493): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


