A0A2Z6E110 · A0A2Z6E110_HYDTE
- ProteinThiol:disulfide interchange protein DsbD
- GenedsbD
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids656 (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 + H+ + NADH
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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Hydrogenophilia > Hydrogenophilales > Hydrogenophilaceae > Hydrogenophilus
Accessions
- Primary accessionA0A2Z6E110
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 | 239-267 | Helical | ||||
Sequence: LAAFFGFGLLLAFTPCVFPMIPILSGIIV | ||||||
Transmembrane | 279-303 | Helical | ||||
Sequence: LGLTLTYVLAMAITYALAGVAAGLS | ||||||
Transmembrane | 315-337 | Helical | ||||
Sequence: AVLVTFALLFVALALSLFGFYEL | ||||||
Transmembrane | 358-388 | Helical | ||||
Sequence: QLIGVAVMGVLSALIVGPCVAPPLVGALLYV | ||||||
Transmembrane | 394-417 | Helical | ||||
Sequence: AVFGGVALFALGLGMGAPLIAVGV | ||||||
Transmembrane | 429-449 | Helical | ||||
Sequence: WMNGVKAAMGVVMLALAWWLV | ||||||
Transmembrane | 455-476 | Helical | ||||
Sequence: DLWWLVGWAVLAVGTAVALGAL | ||||||
Transmembrane | 488-509 | Helical | ||||
Sequence: RMGKALGLLLLAYGVAAFWGAL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MPRRLARGVLAALLFGALSFASA | ||||||
Chain | PRO_5016470503 | 24-656 | Thiol:disulfide interchange protein DsbD | |||
Sequence: ADPVPPEEAYPAEAYRLDAQTIAVEFTIRRDYYLYRDKIRVEPLTPGLQLGTPTIPPGKRKKDDFFGETEVFYDTLKVTVPVESAPATEAPWRIRVISQGCWNGGVCYPPLEQTLTVADAPPQRSWLGKLVGSVTAPDADAPRSSDSNPPSSTAAPSGTAPSMARASVPTGSATAATAPAPSSTSEPPLARAAAPLTDEAGSLAAFIAQQNRAAVLAAFFGFGLLLAFTPCVFPMIPILSGIIVGQGEAISRVRALGLTLTYVLAMAITYALAGVAAGLSGTMLQAALQHPAVLVTFALLFVALALSLFGFYELQLPPSWQTRLNQLAGSQQGGQLIGVAVMGVLSALIVGPCVAPPLVGALLYVSQTGDAVFGGVALFALGLGMGAPLIAVGVGARALLPKSGPWMNGVKAAMGVVMLALAWWLVRPVVADLWWLVGWAVLAVGTAVALGALEPLPIGARWPKRMGKALGLLLLAYGVAAFWGALAGNRDPLQPLAGFAGGNGGIPTANREALTFQPIRSVKELEARVANSTRPVLVDVRADWCISCIELERYTFTDPQVVALLRNVTLLKMDVTENSERDKAFLRHFQIFGPPALLFFAPGNPEELRQYRVTGFVDGPTFATHLRRWLGQT | ||||||
Disulfide bond | 124↔130 | Redox-active | ||||
Sequence: CWNGGVC | ||||||
Disulfide bond | 254↔376 | Redox-active | ||||
Sequence: CVFPMIPILSGIIVGQGEAISRVRALGLTLTYVLAMAITYALAGVAAGLSGTMLQAALQHPAVLVTFALLFVALALSLFGFYELQLPPSWQTRLNQLAGSQQGGQLIGVAVMGVLSALIVGPC | ||||||
Disulfide bond | 568↔571 | Redox-active | ||||
Sequence: CISC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 24-140 | Thiol:disulfide interchange protein DsbD N-terminal | ||||
Sequence: ADPVPPEEAYPAEAYRLDAQTIAVEFTIRRDYYLYRDKIRVEPLTPGLQLGTPTIPPGKRKKDDFFGETEVFYDTLKVTVPVESAPATEAPWRIRVISQGCWNGGVCYPPLEQTLTV | ||||||
Region | 158-215 | Disordered | ||||
Sequence: TAPDADAPRSSDSNPPSSTAAPSGTAPSMARASVPTGSATAATAPAPSSTSEPPLARA | ||||||
Compositional bias | 163-207 | Polar residues | ||||
Sequence: DAPRSSDSNPPSSTAAPSGTAPSMARASVPTGSATAATAPAPSST | ||||||
Domain | 243-444 | Cytochrome C biogenesis protein transmembrane | ||||
Sequence: FGFGLLLAFTPCVFPMIPILSGIIVGQGEAISRVRALGLTLTYVLAMAITYALAGVAAGLSGTMLQAALQHPAVLVTFALLFVALALSLFGFYELQLPPSWQTRLNQLAGSQQGGQLIGVAVMGVLSALIVGPCVAPPLVGALLYVSQTGDAVFGGVALFALGLGMGAPLIAVGVGARALLPKSGPWMNGVKAAMGVVMLAL |
Sequence similarities
Belongs to the thioredoxin family. DsbD subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length656
- Mass (Da)69,220
- Last updated2018-10-10 v1
- ChecksumFD1B257BB163826F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 163-207 | Polar residues | ||||
Sequence: DAPRSSDSNPPSSTAAPSGTAPSMARASVPTGSATAATAPAPSST |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP018558 EMBL· GenBank· DDBJ | BBD78280.1 EMBL· GenBank· DDBJ | Genomic DNA |