Reviewed,
UniProtKB/Swiss-Prot Q7MZX2 (DSBD_PHOLL)
Last modified
June 16, 2009.
Version 48.
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 | Photorhabdus luminescens subsp. laumondii [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 141679 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus |
Protein attributes
| Sequence length | 575 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 – 24 | 24 | Potential | ||||||||
| Chain | 25 – 575 | 551 | Thiol:disulfide interchange protein dsbD HAMAP MF_00399 | PRO_0000304391 | |||||||
Regions | |||||||||||
| Transmembrane | 180 – 200 | 21 | Potential | ||||||||
| Transmembrane | 216 – 236 | 21 | Potential | ||||||||
| Transmembrane | 253 – 273 | 21 | Potential | ||||||||
| Transmembrane | 297 – 317 | 21 | Potential | ||||||||
| Transmembrane | 336 – 356 | 21 | Potential | ||||||||
| Transmembrane | 367 – 387 | 21 | Potential | ||||||||
| Transmembrane | 394 – 414 | 21 | Potential | ||||||||
| Transmembrane | 425 – 445 | 21 | Potential | ||||||||
| Domain | 444 – 575 | 132 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 126 ↔ 132 | Redox-active By similarity | |||||||||
| Disulfide bond | 192 ↔ 314 | Redox-active By similarity | |||||||||
| Disulfide bond | 490 ↔ 493 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens." Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K. Kunst F.Nat. Biotechnol. 21:1307-1313(2003) [PubMed: 14528314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TT01. |
Cross-references
Sequence databases | |
|---|---|
| BX571872 Genomic DNA. Translation: CAE16511.1. | |
| RefSeq | NP_931329.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JPE based on UniProtKB P36655. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2804151. |
| GenomeReviews | Gene locus plu4139 in contig BX470251_GR. |
| KEGG | plu:plu4139. |
| NMPDR | fig|243265.1.peg.3952. |
Organism-specific databases | |
| PhotoList | plu4139. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q7MZX2. |
| OMA | Q7MZX2. TITHILW. |
Enzyme and pathway databases | |
| BioCyc | PLUM243265:PLU4139-MON. |
| BRENDA | 1.8.1.8. 308689. |
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_PHOLL | ||||||||
| Accession | Primary (citable) accession number: Q7MZX2 | ||||||||
| 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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