Reviewed,
UniProtKB/Swiss-Prot Q9I104 (DSBD2_PSEAE)
Last modified
June 16, 2009.
Version 61.
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 2 EC=1.8.1.8 Alternative name(s): Protein-disulfide reductase 2 Short name=Disulfide reductase 2 | ||||
| Gene names |
| ||||
| Organism | Pseudomonas aeruginosa [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 287 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 587 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 | Involved in the formation of correct disulfide bonds in some periplasmic proteins and in 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 – 18 | 18 | Potential | ||||||||
| Chain | 19 – 587 | 569 | Thiol:disulfide interchange protein dsbD 2 HAMAP MF_00399 | PRO_0000007382 | |||||||
Regions | |||||||||||
| Topological domain | 19 – 172 | 154 | Periplasmic Potential | ||||||||
| Transmembrane | 173 – 193 | 21 | Potential | ||||||||
| Topological domain | 194 – 216 | 23 | Cytoplasmic Potential | ||||||||
| Transmembrane | 217 – 237 | 21 | Potential | ||||||||
| Topological domain | 238 – 246 | 9 | Periplasmic Potential | ||||||||
| Transmembrane | 247 – 267 | 21 | Potential | ||||||||
| Topological domain | 268 – 299 | 32 | Cytoplasmic Potential | ||||||||
| Transmembrane | 300 – 320 | 21 | Potential | ||||||||
| Topological domain | 321 – 330 | 10 | Periplasmic Potential | ||||||||
| Transmembrane | 331 – 351 | 21 | Potential | ||||||||
| Topological domain | 352 – 360 | 9 | Cytoplasmic Potential | ||||||||
| Transmembrane | 361 – 381 | 21 | Potential | ||||||||
| Topological domain | 382 – 383 | 2 | Periplasmic Potential | ||||||||
| Transmembrane | 384 – 404 | 21 | Potential | ||||||||
| Topological domain | 405 – 416 | 12 | Cytoplasmic Potential | ||||||||
| Transmembrane | 417 – 437 | 21 | Potential | ||||||||
| Topological domain | 438 – 587 | 150 | Periplasmic Potential | ||||||||
| Domain | 448 – 585 | 138 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 124 ↔ 130 | Redox-active By similarity | |||||||||
| Disulfide bond | 188 ↔ 308 | Redox-active By similarity | |||||||||
| Disulfide bond | 500 ↔ 503 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
Cross-references
Sequence databases | |
|---|---|
| AE004091 Genomic DNA. Translation: AAG05866.1. | |
| PIR | F83336. |
| RefSeq | NP_251168.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JPE based on UniProtKB P36655. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 882175. |
| GenomeReviews | Gene locus PA2478 in contig AE004091_GR. |
| KEGG | pae:PA2478. |
| NMPDR | fig|208964.1.peg.2478. |
Organism-specific databases | |
| PseudoCAP | PA2478. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9I104. |
| OMA | Q9I104. LQQPWLL. |
Enzyme and pathway databases | |
| BioCyc | PAER208964:PA2478-MON. |
| BRENDA | 1.8.1.8. 354. |
Family and domain databases | |
| HAMAP | MF_00399. [Tree] |
| InterPro | IPR003834. Cyt_c_assmbl_TM. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| Pfam | PF02683. DsbD. 1 hit. [Graphical view] |
| PROSITE | PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DSBD2_PSEAE | ||||||||
| Accession | Primary (citable) accession number: Q9I104 | ||||||||
| 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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