Reviewed,
UniProtKB/Swiss-Prot Q7VMZ4 (DSBD_HAEDU)
Last modified
June 16, 2009.
Version 47.
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 |
| ||||
| Organism | Haemophilus ducreyi [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 730 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 573 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 – 20 | 20 | Potential | ||||||||
| Chain | 21 – 573 | 553 | Thiol:disulfide interchange protein dsbD HAMAP MF_00399 | PRO_0000007375 | |||||||
Regions | |||||||||||
| Topological domain | 21 – 175 | 155 | Periplasmic Potential | ||||||||
| Transmembrane | 176 – 196 | 21 | Potential | ||||||||
| Topological domain | 197 – 227 | 31 | Cytoplasmic Potential | ||||||||
| Transmembrane | 228 – 248 | 21 | Potential | ||||||||
| Topological domain | 249 – 251 | 3 | Periplasmic Potential | ||||||||
| Transmembrane | 252 – 272 | 21 | Potential | ||||||||
| Topological domain | 273 – 292 | 20 | Cytoplasmic Potential | ||||||||
| Transmembrane | 293 – 313 | 21 | Potential | ||||||||
| Topological domain | 314 – 331 | 18 | Periplasmic Potential | ||||||||
| Transmembrane | 332 – 352 | 21 | Potential | ||||||||
| Topological domain | 353 – 365 | 13 | Cytoplasmic Potential | ||||||||
| Transmembrane | 366 – 386 | 21 | Potential | ||||||||
| Topological domain | 387 – 393 | 7 | Periplasmic Potential | ||||||||
| Transmembrane | 394 – 414 | 21 | Potential | ||||||||
| Topological domain | 415 – 425 | 11 | Cytoplasmic Potential | ||||||||
| Transmembrane | 426 – 446 | 21 | Potential | ||||||||
| Topological domain | 447 – 573 | 127 | Periplasmic Potential | ||||||||
| Domain | 440 – 573 | 134 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 121 ↔ 126 | Redox-active By similarity | |||||||||
| Disulfide bond | 191 ↔ 313 | Redox-active By similarity | |||||||||
| Disulfide bond | 490 ↔ 493 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "The complete genome sequence of Haemophilus ducreyi." Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L. Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 35000HP / ATCC 700724. |
Cross-references
Sequence databases | |
|---|---|
| AE017143 Genomic DNA. Translation: AAP95707.1. | |
| RefSeq | NP_873318.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JPE based on UniProtKB P36655. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1490764. |
| GenomeReviews | Gene locus HD_0807 in contig AE017143_GR. |
| KEGG | hdu:HD0807. |
| NMPDR | fig|233412.1.peg.683. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q7VMZ4. |
| OMA | Q7VMZ4. LQQPWLL. |
Enzyme and pathway databases | |
| BioCyc | HDUC233412:HD_0807-MON. |
| BRENDA | 1.8.1.8. 265031. |
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_HAEDU | ||||||||
| Accession | Primary (citable) accession number: Q7VMZ4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


