O32823 (TRXB_LISMO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 85.
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: Thioredoxin reductase Short name=TRXR EC=1.8.1.9 | ||||
| Gene names |
| ||||
| Organism | Listeria monocytogenes | ||||
| Taxonomic identifier | 1639 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria |
Protein attributes
| Sequence length | 319 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological process | removal of superoxide radicals Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | flavin adenine dinucleotide 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 – 319 | 319 | Thioredoxin reductase | PRO_0000166736 | |||||||
Regions | |||||||||||
| Nucleotide binding | 37 – 44 | 8 | FAD By similarity | ||||||||
| Nucleotide binding | 279 – 288 | 10 | FAD By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 136 ↔ 139 | Redox-active By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation, cloning and characterization of the Listeria monocytogenes thioredoxin reductase gene, trxB." Borovok I., Mislovati M., Cohen G., Aharonowitz Y. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: EGD / Serovar 1/2a. |
| [2] | "Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. Cossart P.Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e / Serovar 1/2a. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF009622 Genomic DNA. Translation: AAB63804.1. AL591983 Genomic DNA. Translation: CAD00556.1. |
| PIR | AF1384. |
| RefSeq | NP_466001.1. NC_003210.1. |
3D structure databases | |
| ProteinModelPortal | O32823. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 987338. |
| GenomeReviews | Gene locus lmo2478 in contig AL591824_GR. |
| KEGG | lmo:lmo2478. |
| PATRIC | 20314233. VBILisMon69206_2538. |
Organism-specific databases | |
| GenoList | LMO2478. |
Phylogenomic databases | |
| HOGENOM | HBG669726. |
| OMA | GEEREFP. |
| ProtClustDB | CLSK2753262. |
Enzyme and pathway databases | |
| BioCyc | LMON169963:LMO2478-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] |
| 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 | TRXB_LISMO | ||||||||
| Accession | Primary (citable) accession number: O32823 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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