Reviewed,
UniProtKB/Swiss-Prot P44919 (DSBD_HAEIN)
Last modified
June 16, 2009.
Version 72.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 C-type cytochrome biogenesis protein cycZ | ||||||
| Gene names |
| ||||||
| Organism | Haemophilus influenzae [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 727 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 579 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 – 16 | 16 | Potential | ||||||||
| Chain | 17 – 579 | 563 | Thiol:disulfide interchange protein dsbD HAMAP MF_00399 | PRO_0000007376 | |||||||
Regions | |||||||||||
| Topological domain | 17 – 177 | 161 | Periplasmic Potential | ||||||||
| Transmembrane | 178 – 198 | 21 | Potential | ||||||||
| Topological domain | 199 – 229 | 31 | Cytoplasmic Potential | ||||||||
| Transmembrane | 230 – 250 | 21 | Potential | ||||||||
| Topological domain | 251 – 253 | 3 | Periplasmic Potential | ||||||||
| Transmembrane | 254 – 274 | 21 | Potential | ||||||||
| Topological domain | 275 – 295 | 21 | Cytoplasmic Potential | ||||||||
| Transmembrane | 296 – 316 | 21 | Potential | ||||||||
| Topological domain | 317 – 336 | 20 | Periplasmic Potential | ||||||||
| Transmembrane | 337 – 357 | 21 | Potential | ||||||||
| Topological domain | 358 – 367 | 10 | Cytoplasmic Potential | ||||||||
| Transmembrane | 368 – 388 | 21 | Potential | ||||||||
| Topological domain | 389 – 396 | 8 | Periplasmic Potential | ||||||||
| Transmembrane | 397 – 417 | 21 | Potential | ||||||||
| Topological domain | 418 – 419 | 2 | Cytoplasmic Potential | ||||||||
| Transmembrane | 420 – 440 | 21 | Potential | ||||||||
| Topological domain | 441 – 579 | 139 | Periplasmic Potential | ||||||||
| Domain | 449 – 579 | 131 | Thioredoxin | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 124 ↔ 129 | Redox-active By similarity | |||||||||
| Disulfide bond | 193 ↔ 315 | Redox-active By similarity | |||||||||
| Disulfide bond | 495 ↔ 498 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
Cross-references
Sequence databases | |
|---|---|
| L42023 Genomic DNA. Translation: AAC22543.1. | |
| PIR | A64100. |
| RefSeq | NP_439046.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1JPE based on UniProtKB P36655. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 950312. |
| GenomeReviews | Gene locus HI0885 in contig L42023_GR. |
| KEGG | hin:HI0885. |
| NMPDR | fig|71421.1.peg.852. |
| TIGR | HI0885. |
Phylogenomic databases | |
| HOGENOM | P44919. |
| OMA | P44919. PVFLLSR. |
Enzyme and pathway databases | |
| BioCyc | HINF71421:HI_0885-MON. |
| BRENDA | 1.8.1.8. 109. |
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_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P44919 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


