D2TU38 (D2TU38_CITRI) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 26.
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 | Submitted name: Thioredoxin 2 EMBL CBG89270.1 EC=1.8.1.8 EMBL CBG89270.1 | ||||
| Gene names |
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| Organism | Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280) [Complete proteome] [HAMAP] EMBL CBG89270.1 | ||||
| Taxonomic identifier | 637910 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Citrobacter › ![]() |
Protein attributes
| Sequence length | 171 AA. |
| Sequence status | Complete. |
| Protein existence | Predicted |
General annotation (Comments)
| Sequence similarities | Contains 1 thioredoxin domain. RuleBase RU004207 |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Oxidoreductase EMBL CBG89270.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro glycerol ether metabolic processInferred from electronic annotation. Source: InterPro |
| Molecular_function | electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activityInferred from electronic annotation. Source: InterPro protein-disulfide reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequences
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References
| [1] | "The Citrobacter rodentium genome sequence reveals convergent evolution with human pathogenic Escherichia coli." Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G., Thomson N.R. J. Bacteriol. 192:525-538(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ICC168 EMBL CBG89270.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FN543502 Genomic DNA. Translation: CBG89270.1. |
| RefSeq | YP_003366062.1. NC_013716.1. |
3D structure databases | |
| ProteinModelPortal | D2TU38. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CBG89270; CBG89270; ROD_25271. |
| GeneID | 8711298. |
| KEGG | cro:ROD_25271. |
| PATRIC | 32028875. VBICitRod33214_2452. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000292979. |
| KO | K03672. |
| OMA | IVCPHCH. |
Enzyme and pathway databases | |
| BioCyc | CROD637910:GJIG-2553-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.30.10. 1 hit. |
| InterPro | IPR005746. Thioredoxin. IPR012336. Thioredoxin-like_fold. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. [Graphical view] |
| PANTHER | PTHR10438. PTHR10438. 1 hit. |
| Pfam | PF00085. Thioredoxin. 1 hit. [Graphical view] |
| PRINTS | PR00421. THIOREDOXIN. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| TIGRFAMs | TIGR01068. thioredoxin. 1 hit. |
| PROSITE | PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | D2TU38_CITRI | ||||||||
| Accession | Primary (citable) accession number: D2TU38 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
