Reviewed,
UniProtKB/Swiss-Prot O05542 (DHET_GLUOX)
Last modified
June 16, 2009.
Version 81.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alcohol dehydrogenase [acceptor] EC=1.1.99.8 Alternative name(s): G3-ADH subunit I | ||||
| Gene names |
| ||||
| Organism | Gluconobacter oxydans (Gluconobacter suboxydans) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 442 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter |
Protein attributes
| Sequence length | 757 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)
| Function | Dehydration of primary alcohols (exception: methanol) By similarity. |
| Catalytic activity | A primary alcohol + acceptor = an aldehyde + reduced acceptor. |
| Cofactor | Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-141-Cys-142 and the indole ring of Trp-279 By similarity. Binds 1 calcium ion per subunit By similarity. Binds 1 heme group per subunit By similarity. |
| Subunit structure | Heterotrimer (dehydrogenase, cytochrome and protein adhS), that forms the alcohol dehydrogenase complex. |
| Subcellular location | Cell membrane; Peripheral membrane protein; Periplasmic side Potential. |
| Sequence similarities | Belongs to the bacterial PQQ dehydrogenase family. Contains 1 cytochrome c domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Signal |
| Ligand | Calcium Heme Iron Metal-binding |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond PQQ Pyrrolidone carboxylic acid |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | outer membrane-bounded periplasmic space Inferred from electronic annotation. Source: InterPro plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| 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 – 34 | 34 | |||||||||
| Chain | 35 – 757 | 723 | Alcohol dehydrogenase [acceptor] | PRO_0000025562 | |||||||
Regions | |||||||||||
| Domain | 637 – 726 | 90 | Cytochrome c | ||||||||
Sites | |||||||||||
| Active site | 342 | 1 | Proton acceptor Potential | ||||||||
| Metal binding | 215 | 1 | Calcium By similarity | ||||||||
| Metal binding | 297 | 1 | Calcium By similarity | ||||||||
| Metal binding | 657 | 1 | Iron (heme axial ligand) By similarity | ||||||||
| Binding site | 653 | 1 | Heme (covalent) By similarity | ||||||||
| Binding site | 656 | 1 | Heme (covalent) By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 35 | 1 | Pyrrolidone carboxylic acid | ||||||||
| Disulfide bond | 141 ↔ 142 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 230 | 1 | G → S in BAA19753. Ref.1 | ||||||||
| Sequence conflict | 675 | 1 | A → R in BAA19753. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Characterization of the genes encoding the three-component membrane-bound alcohol dehydrogenase from Gluconobacter suboxydans and their expression in Acetobacter pasteurianus." Kondo K., Horinouchi S. Appl. Environ. Microbiol. 63:1131-1138(1997) [PubMed: 9055427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-50. Strain: ATCC 621 / IFO 3172 / NCIB 7069. |
| [2] | "Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans." Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U. Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 621H. |
Cross-references
Sequence databases | |
|---|---|
| D86375 Genomic DNA. Translation: BAA19753.1. CP000009 Genomic DNA. Translation: AAW60837.1. | |
| RefSeq | YP_191493.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1KB0 based on UniProtKB Q46444. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3250283. |
| GenomeReviews | Gene locus GOX1068 in contig CP000009_GR. |
| KEGG | gox:GOX1068. |
| NMPDR | fig|290633.1.peg.1038. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O05542. |
| OMA | O05542. MYVTASW. |
Enzyme and pathway databases | |
| BioCyc | GOXY290633:GOX1068-MON. |
| BRENDA | 1.1.99.8. 3050. |
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. [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. 6 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. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHET_GLUOX | ||||||||
| Accession | Primary (citable) accession number: O05542 Secondary accession number(s): Q5FS09 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


