Reviewed,
UniProtKB/Swiss-Prot A7MMC7 (DSBD_ENTS8)
Last modified
June 16, 2009.
Version 16.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Thiol:disulfide interchange protein dsbD EC=1.8.1.8 Alternative name(s): Protein-disulfide reductase Short name=Disulfide reductase | ||||
| Gene names |
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| Organism | Enterobacter sakazakii (strain ATCC BAA-894) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 290339 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Cronobacter |
Protein attributes
| Sequence length | 574 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps By similarity. |
| Catalytic activity | Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. HAMAP MF_00399 |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the thioredoxin family. DsbD subfamily. Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cytochrome c-type biogenesis Electron transport Transport |
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Redox-active center Signal Transmembrane |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro cytochrome complex assemblyInferred from electronic annotation. Source: HAMAP electron transport chainInferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: HAMAP protein-disulfide reductase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||||
| Chain | 20 – 574 | 555 | Thiol:disulfide interchange protein dsbD HAMAP MF_00399 | PRO_1000049608 | |||||||
Regions | |||||||||||
| Transmembrane | 173 – 193 | 21 | Potential | ||||||||
| Transmembrane | 218 – 238 | 21 | Potential | ||||||||
| Transmembrane | 253 – 273 | 21 | Potential | ||||||||
| Transmembrane | 306 – 326 | 21 | Potential | ||||||||
| Transmembrane | 333 – 353 | 21 | Potential | ||||||||
| Transmembrane | 367 – 387 | 21 | Potential | ||||||||
| Transmembrane | 399 – 419 | 21 | Potential | ||||||||
| Domain | 430 – 574 | 145 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 122 ↔ 128 | Redox-active By similarity | |||||||||
| Disulfide bond | 192 ↔ 314 | Redox-active By similarity | |||||||||
| Disulfide bond | 489 ↔ 492 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., Fulton B., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., Johnson M., Thiruvilangam P., Wilson R. Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000783 Genomic DNA. Translation: ABU75452.1. | |
| RefSeq | YP_001436288.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5549371. |
| GenomeReviews | Gene locus ESA_00148 in contig CP000783_GR. |
| KEGG | esa:ESA_00148. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | A7MMC7. HTDEYFG. |
Family and domain databases | |
| HAMAP | MF_00399. [Tree] |
| InterPro | IPR003834. Cyt_c_assmbl_TM. IPR017936. Thioredoxin-like. IPR015467. Thioredoxin_core. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| PANTHER | PTHR10438. Trx. 1 hit. |
| Pfam | PF02683. DsbD. 1 hit. PF00085. Thioredoxin. 1 hit. [Graphical view] |
| PROSITE | PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DSBD_ENTS8 | ||||||||
| Accession | Primary (citable) accession number: A7MMC7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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