A2RLJ5 (A2RLJ5_LACLM) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 38.
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 | Lactococcus lactis subsp. cremoris (strain MG1363) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 416870 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Streptococcaceae › Lactococcus |
Protein attributes
| Sequence length | 308 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 CAL98163.1 |
| 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] | "The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363." Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J. J. Bacteriol. 189:3256-3270(2007) [PubMed: 17307855] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM406671 Genomic DNA. Translation: CAL98163.1. |
| RefSeq | YP_001032873.1. NC_009004.1. |
3D structure databases | |
| ProteinModelPortal | A2RLJ5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A2RLJ5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4798271. |
| GenomeReviews | Gene locus llmg_1588 in contig AM406671_GR. |
| KEGG | llm:llmg_1588. |
| PATRIC | 22284346. VBILacLac4574_1628. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0492. |
| HOGENOM | HBG669726. |
| OMA | AVEEAMY. |
| ProtClustDB | CLSK2458888. |
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 | A2RLJ5_LACLM | ||||||||
| Accession | Primary (citable) accession number: A2RLJ5 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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