Reviewed,
UniProtKB/Swiss-Prot P27175 (DHG_GLUOX)
Last modified
June 16, 2009.
Version 67.
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: Quinoprotein glucose dehydrogenase EC=1.1.5.2 Alternative name(s): Glucose dehydrogenase [pyrroloquinoline-quinone] | ||||
| 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 | 808 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol. |
| Cofactor | PQQ. |
| Subcellular location | Cell inner membrane; Multi-pass membrane protein; Periplasmic side. |
| Miscellaneous | The P1 form can oxidize only D-glucose, while the P2 form can also oxidize maltose. The sequence of P1 form is shown here. |
| Sequence similarities | Belongs to the bacterial PQQ dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell inner membrane Cell membrane Membrane |
| Domain | Signal Transmembrane |
| Molecular function | Oxidoreductase |
| PTM | PQQ |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW outer membrane-bounded periplasmic spaceInferred from electronic annotation. Source: InterPro plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro quinone bindingInferred from electronic annotation. Source: InterPro quinoprotein glucose dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 33 | 33 | Potential | ||||||
| Chain | 34 – 808 | 775 | Quinoprotein glucose dehydrogenase | PRO_0000025558 | |||||
Regions | |||||||||
| Transmembrane | 35 – 54 | 20 | Potential | ||||||
| Transmembrane | 59 – 76 | 18 | Potential | ||||||
| Transmembrane | 94 – 108 | 15 | Potential | ||||||
| Transmembrane | 123 – 138 | 16 | Potential | ||||||
Sites | |||||||||
| Active site | 470 | 1 | Proton acceptor Potential | ||||||
Natural variations | |||||||||
| Natural variant | 788 | 1 | H → N in P2 form. | ||||||
Experimental info | |||||||||
| Sequence conflict | 4 | 1 | T → I in CAA44594. Ref.1 | ||||||
| Sequence conflict | 8 | 1 | G → R in CAA44594. Ref.1 | ||||||
| Sequence conflict | 110 – 123 | 14 | QIGGT…LPLAG → ARSVARGRPSCRSP Ref.1 | ||||||
| Sequence conflict | 146 | 1 | D → E in CAA44594. Ref.1 | ||||||
| Sequence conflict | 188 | 1 | S → T in CAA44594. Ref.1 | ||||||
| Sequence conflict | 213 | 1 | A → Q Ref.1 | ||||||
| Sequence conflict | 277 | 1 | T → M in CAA44594. Ref.1 | ||||||
| Sequence conflict | 291 – 292 | 2 | RI → DS in CAA44594. Ref.1 | ||||||
| Sequence conflict | 395 | 1 | D → E in CAA44594. Ref.1 | ||||||
| Sequence conflict | 415 | 1 | R → A in CAA44594. Ref.1 | ||||||
| Sequence conflict | 472 – 473 | 2 | DV → EL in CAA44594. Ref.1 | ||||||
| Sequence conflict | 635 – 636 | 2 | KD → EN in CAA44594. Ref.1 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "A single amino acid substitution changes the substrate specificity of quinoprotein glucose dehydrogenase in Gluconobacter oxydans." Cleton-Jansen A.-M., Dekker S., van de Putte P., Goosen N. Mol. Gen. Genet. 229:206-212(1991) [PubMed: 1833618] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | Goosen N. Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 213. |
| [3] | "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 | |
|---|---|
| X62710 Genomic DNA. Translation: CAA44594.1. Sequence problems. CP000009 Genomic DNA. Translation: AAW60048.1. | |
| PIR | QPKEX. S17716. |
| RefSeq | YP_190704.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3248643. |
| GenomeReviews | Gene locus GOX0265 in contig CP000009_GR. |
| KEGG | gox:GOX0265. |
| NMPDR | fig|290633.1.peg.249. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P27175. |
| OMA | P27175. LTGADMW. |
Enzyme and pathway databases | |
| BioCyc | GOXY290633:GOX0265-MON. |
| BRENDA | 1.1.5.2. 3050. |
Family and domain databases | |
| InterPro | IPR017511. PQQ-dep_membr-bd_DH. IPR019556. PQQ-dependent_C. IPR019551. PQQ-dependent_N. IPR018391. PQQ_beta_propeller_repeat. IPR002372. PQQ_repeat. IPR011047. Quino_AlcDH-like. IPR001479. Quinoprotein_DH_CS. [Graphical view] |
| Gene3D | 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. 3 hits. [Graphical view] |
| TIGRFAMs | TIGR03074. PQQ_membr_DH. 1 hit. |
| PROSITE | PS00363. BACTERIAL_PQQ_1. 1 hit. PS00364. BACTERIAL_PQQ_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHG_GLUOX | ||||||||
| Accession | Primary (citable) accession number: P27175 Secondary accession number(s): Q5FU98 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


