Reviewed,
UniProtKB/Swiss-Prot P18278 (DHET_ACEAC)
Last modified
June 16, 2009.
Version 76.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Alcohol dehydrogenase [acceptor] EC=1.1.99.8 | ||||
| Gene names |
| ||||
| Organism | Acetobacter aceti | ||||
| Taxonomic identifier | 435 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acetobacter › Acetobacter subgen. Acetobacter |
Protein attributes
| Sequence length | 742 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | A primary alcohol + acceptor = an aldehyde + reduced acceptor. |
| Cofactor | Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-142-Cys-143 and the indole ring of Trp-280 By similarity. Binds 1 calcium ion per subunit By similarity. Binds 1 heme group per subunit By similarity. |
| Subunit structure | Tetramer of non identical chains (dehydrogenase, cytochrome, and two smaller unknown subunits). |
| Subcellular location | |
| Sequence similarities | Belongs to the bacterial PQQ dehydrogenase family. Contains 1 cytochrome c domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Periplasm |
| Domain | Signal |
| Ligand | Calcium Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond PQQ |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | membrane Inferred from electronic annotation. Source: InterPro outer membrane-bounded periplasmic spaceInferred from electronic annotation. Source: InterPro |
| Molecular function | alcohol dehydrogenase (acceptor) activity Inferred from electronic annotation. Source: EC calcium ion bindingInferred from electronic annotation. Source: UniProtKB-KW electron carrier activityInferred from electronic annotation. Source: InterPro heme bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 35 | 35 | Ref.1 | ||||||||
| Chain | 36 – 742 | 707 | Alcohol dehydrogenase [acceptor] | PRO_0000025559 | |||||||
Regions | |||||||||||
| Domain | 633 – 742 | 110 | Cytochrome c | ||||||||
Sites | |||||||||||
| Active site | 343 | 1 | Proton acceptor Potential | ||||||||
| Metal binding | 216 | 1 | Calcium By similarity | ||||||||
| Metal binding | 298 | 1 | Calcium By similarity | ||||||||
| Metal binding | 653 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Binding site | 649 | 1 | Heme (covalent) By similarity | ||||||||
| Binding site | 652 | 1 | Heme (covalent) By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 142 ↔ 143 | By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Cloning and sequencing of the gene encoding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti." Inoue T., Sunagawa M., Mori A., Imai C., Fukuda M., Takagi M., Yano K. J. Bacteriol. 171:3115-3122(1989) [PubMed: 2722742] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-50. |
| [2] | "The structure of the quinoprotein alcohol dehydrogenase of Acetobacter aceti modelled on that of methanol dehydrogenase from Methylobacterium extorquens." Cozier G.E., Giles I.G., Anthony C. Biochem. J. 308:375-379(1995) [PubMed: 7772016] [Abstract] Cited for: 3D-STRUCTURE MODELING. |
Cross-references
Sequence databases | |
|---|---|
| D90004 Genomic DNA. Translation: BAA14058.1. | |
| PIR | JS0326. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KB0 based on UniProtKB Q46444. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.1.99.8. 273. |
Family and domain databases | |
| InterPro | IPR009056. Cyt_c_monohaem. IPR019556. PQQ-dependent_C. IPR019551. PQQ-dependent_N. IPR018391. PQQ_beta_propeller_repeat. IPR017512. PQQ_MeOH/EtOH_DH. IPR002372. PQQ_repeat. IPR011047. Quino_AlcDH-like. IPR001479. Quinoprotein_DH_CS. IPR017909. Twin_arg_translocation_Tat. [Graphical view] |
| Gene3D | G3DSA:1.10.760.10. Cytochrome_c_R. 1 hit. G3DSA:2.140.10.10. Quinoprotein_alc_DH-like. 1 hit. |
| Pfam | PF01011. PQQ. 6 hits. PF10535. PQQ_C. 1 hit. PF10527. PQQ_N. 1 hit. [Graphical view] |
| SMART | SM00564. PQQ. 5 hits. [Graphical view] |
| TIGRFAMs | TIGR03075. PQQ_enz_alc_DH. 1 hit. |
| PROSITE | PS00363. BACTERIAL_PQQ_1. 1 hit. PS00364. BACTERIAL_PQQ_2. 1 hit. PS51007. CYTC. 1 hit. PS51318. TAT. 1 hit. Uncertain. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHET_ACEAC | ||||||||
| Accession | Primary (citable) accession number: P18278 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


