D8GNH2 (D8GNH2_CLOLD) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 18.
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 | Clostridium ljungdahlii (strain ATCC 55383 / DSM 13528 / PETC) [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 748727 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › ![]() |
Protein attributes
| Sequence length | 315 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 ADK15835.1 |
| 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] | "Clostridium ljungdahlii represents a microbial production platform based on syngas." Kopke M., Held C., Hujer S., Liesegang H., Wiezer A., Wollherr A., Ehrenreich A., Liebl W., Gottschalk G., Durre P. Proc. Natl. Acad. Sci. U.S.A. 107:13087-13092(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 55383 / DSM 13528 / PETC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001666 Genomic DNA. Translation: ADK15835.1. |
| RefSeq | YP_003780937.1. NC_014328.1. |
3D structure databases | |
| ProteinModelPortal | D8GNH2. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADK15835; ADK15835; CLJU_c27810. |
| GeneID | 9446397. |
| KEGG | clj:CLJU_c27810. |
| PATRIC | 42486895. VBICloLju82977_2813. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000072911. |
| KO | K00384. |
Enzyme and pathway databases | |
| BioCyc | CLJU748727:GHMO-2780-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 | D8GNH2_CLOLD | ||||||||
| Accession | Primary (citable) accession number: D8GNH2 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
