A0A8T6ZM05 · A0A8T6ZM05_9BURK
- ProteinThiol:disulfide interchange protein DsbD
- GenedsbD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids657 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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.
Catalytic activity
- [protein]-dithiol + NAD+ = [protein]-disulfide + NADH + H+
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | electron transfer activity | |
Molecular Function | protein-disulfide reductase (NAD(P)H) activity | |
Biological Process | cell redox homeostasis | |
Biological Process | cytochrome complex assembly |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThiol:disulfide interchange protein DsbD
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Paraburkholderia
Accessions
- Primary accessionA0A8T6ZM05
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 209-242 | Helical | ||||
Sequence: GFFGVVGLYFLAGVVLSLLPCSYPMIPILSAIIV | ||||||
Transmembrane | 254-278 | Helical | ||||
Sequence: FALSFVYVLGMALVYTVLGIAAALV | ||||||
Transmembrane | 290-313 | Helical | ||||
Sequence: WVLGVFAGLLTAFALMLIAGYDLA | ||||||
Transmembrane | 334-364 | Helical | ||||
Sequence: FAAVAVMGALSALVAGACMTAPLFAVLAFIA | ||||||
Transmembrane | 370-398 | Helical | ||||
Sequence: VLGGAALFAMGIGLGVPLMIIGLGAGTLL | ||||||
Transmembrane | 410-428 | Helical | ||||
Sequence: VFFGIALLAAALWIVWPVL | ||||||
Transmembrane | 434-452 | Helical | ||||
Sequence: MLLAALWLLLAAAALGLFT | ||||||
Transmembrane | 464-485 | Helical | ||||
Sequence: LGRGVGAAFAIWAATLIVGLSA |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 138↔144 | Redox-active | ||||
Sequence: CADAGIC | ||||||
Disulfide bond | 229↔351 | Redox-active | ||||
Sequence: CSYPMIPILSAIIVGEGAQVTRARGFALSFVYVLGMALVYTVLGIAAALVGQSLGAWLQNPWVLGVFAGLLTAFALMLIAGYDLALPQRWQDGASRASQGRSGGKFAAVAVMGALSALVAGAC | ||||||
Disulfide bond | 551↔554 | Redox-active | ||||
Sequence: CVSC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 506-634 | Thioredoxin | ||||
Sequence: GNGGAQTGAAEADALTFAPVRSSAQLDAMLKTAGKPSMLDFYADWCVSCKEMENLTFSDPRVQARLAQLGLLRADVTANNADDQALLKRFGLFGPPGIIFFDASGQEVLRVVGYENADKFLARLDRVVA | ||||||
Region | 637-657 | Disordered | ||||
Sequence: QSPAPSAKPVQSVLSTLTGRS | ||||||
Compositional bias | 640-657 | Polar residues | ||||
Sequence: APSAKPVQSVLSTLTGRS |
Sequence similarities
Belongs to the thioredoxin family. DsbD subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length657
- Mass (Da)68,378
- Last updated2022-10-12 v1
- ChecksumCFB5F2E2206A7A81
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 640-657 | Polar residues | ||||
Sequence: APSAKPVQSVLSTLTGRS |
Keywords
- Technical term