Reviewed,
UniProtKB/Swiss-Prot Q9CP40 (DSBD_PASMU)
Last modified
June 16, 2009.
Version 56.
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 | Pasteurella multocida [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 747 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella |
Protein attributes
| Sequence length | 576 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 – 576 | 557 | Thiol:disulfide interchange protein dsbD HAMAP MF_00399 | PRO_0000007380 | |||||||
Regions | |||||||||||
| Topological domain | 20 – 177 | 158 | Periplasmic Potential | ||||||||
| Transmembrane | 178 – 198 | 21 | Potential | ||||||||
| Topological domain | 199 – 229 | 31 | Cytoplasmic Potential | ||||||||
| Transmembrane | 230 – 250 | 21 | Potential | ||||||||
| Topological domain | 251 – 253 | 3 | Periplasmic Potential | ||||||||
| Transmembrane | 254 – 274 | 21 | Potential | ||||||||
| Topological domain | 275 – 295 | 21 | Cytoplasmic Potential | ||||||||
| Transmembrane | 296 – 316 | 21 | Potential | ||||||||
| Topological domain | 317 – 336 | 20 | Periplasmic Potential | ||||||||
| Transmembrane | 337 – 357 | 21 | Potential | ||||||||
| Topological domain | 358 – 367 | 10 | Cytoplasmic Potential | ||||||||
| Transmembrane | 368 – 388 | 21 | Potential | ||||||||
| Topological domain | 389 – 394 | 6 | Periplasmic Potential | ||||||||
| Transmembrane | 395 – 415 | 21 | Potential | ||||||||
| Topological domain | 416 – 419 | 4 | Cytoplasmic Potential | ||||||||
| Transmembrane | 420 – 440 | 21 | Potential | ||||||||
| Topological domain | 441 – 576 | 136 | Periplasmic Potential | ||||||||
| Domain | 433 – 570 | 138 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 120 ↔ 125 | Redox-active By similarity | |||||||||
| Disulfide bond | 193 ↔ 315 | Redox-active By similarity | |||||||||
| Disulfide bond | 485 ↔ 488 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Complete genomic sequence of Pasteurella multocida Pm70." May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V. Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed: 11248100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pm70. |
Cross-references
Sequence databases | |
|---|---|
| AE004439 Genomic DNA. Translation: AAK02305.1. Different initiation. | |
| RefSeq | NP_245158.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JPE based on UniProtKB P36655. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1243568. |
| GenomeReviews | Gene locus PM0221 in contig AE004439_GR. |
| KEGG | pmu:PM0221. |
| NMPDR | fig|272843.1.peg.221. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9CP40. |
Enzyme and pathway databases | |
| BRENDA | 1.8.1.8. 258935. |
Family and domain databases | |
| HAMAP | MF_00399. [Tree] |
| InterPro | IPR003834. Cyt_c_assmbl_TM. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 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_PASMU | ||||||||
| Accession | Primary (citable) accession number: Q9CP40 | ||||||||
| 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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