Reviewed,
UniProtKB/Swiss-Prot Q57GQ5 (DSBD_SALCH)
Last modified
June 16, 2009.
Version 38.
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 | Salmonella choleraesuis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 28901 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella |
Protein attributes
| Sequence length | 567 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 – 567 | 548 | Thiol:disulfide interchange protein dsbD HAMAP MF_00399 | PRO_0000304394 | |||||||
Regions | |||||||||||
| Transmembrane | 166 – 186 | 21 | Potential | ||||||||
| Transmembrane | 210 – 230 | 21 | Potential | ||||||||
| Transmembrane | 246 – 266 | 21 | Potential | ||||||||
| Transmembrane | 299 – 319 | 21 | Potential | ||||||||
| Transmembrane | 326 – 346 | 21 | Potential | ||||||||
| Transmembrane | 360 – 380 | 21 | Potential | ||||||||
| Transmembrane | 387 – 407 | 21 | Potential | ||||||||
| Transmembrane | 418 – 438 | 21 | Potential | ||||||||
| Domain | 435 – 567 | 133 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 122 ↔ 128 | Redox-active By similarity | |||||||||
| Disulfide bond | 185 ↔ 307 | Redox-active By similarity | |||||||||
| Disulfide bond | 482 ↔ 485 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly invasive and resistant zoonotic pathogen." Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S., Lee Y.-S. Nucleic Acids Res. 33:1690-1698(2005) [PubMed: 15781495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC-B67. |
Cross-references
Sequence databases | |
|---|---|
| AE017220 Genomic DNA. Translation: AAX68107.1. | |
| RefSeq | YP_219188.1. |
3D structure databases | |
| SMR | Q57GQ5. Positions 23-143, 449-567. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3336750. |
| GenomeReviews | Gene locus SCH_4201 in contig AE017220_GR. |
| KEGG | sec:SC4201. |
| NMPDR | fig|321314.4.peg.4257. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q57GQ5. |
| OMA | Q57GQ5. TITHILW. |
Enzyme and pathway databases | |
| BioCyc | SENT321314:SCH_4201-MON. |
| BRENDA | 1.8.1.8. 276841. |
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_SALCH | ||||||||
| Accession | Primary (citable) accession number: Q57GQ5 | ||||||||
| 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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