| Accession | TIGR03075 |
| Name | PQQ_enz_alc_DH |
| Function | PQQ-dependent dehydrogenase, methanol/ethanol family |
| Trusted Cutoff | 480.05 |
| Domain Trusted Cutoff | 480.05 |
| Noise Cutoff | 249.80 |
| Domain Noise Cutoff | 249.80 |
| Isology Type | subfamily |
| EC Number | 1.1.2.- |
| HMM Length | 530 |
| Gene Ontology Term | GO:0016491: oxidoreductase activity molecular_function |
| | GO:0050662: coenzyme binding molecular_function |
| Author | Haft DH |
| Entry Date | Sep 20 2006 1:12PM |
| Last Modified | Mar 6 2014 3:28PM |
| Comment | This protein family has a phylogenetic distribution very similar to that coenzyme PQQ biosynthesis enzymes, as shown by partial phylogenetic profiling. Genes in this family often are found adjacent to the PQQ biosynthesis genes themselves. An unusual, strained disulfide bond between adjacent Cys residues contributes to PQQ-binding, as does a Trp residue that is part of a PQQ enzyme repeat (see PF01011). Characterized members include the dehydrogenase subunit of a membrane-anchored, three subunit alcohol (ethanol) dehydrogenase of Gluconobacter suboxydans, a homodimeric ethanol dehydrogenase in Pseudomonas aeruginosa, and the large subunit of an alpha2/beta2 heterotetrameric methanol dehydrogenase in Methylobacterium extorquens. |
| References | DR PFAM; PF01011; PQQ enzyme repeat
RN [1]
RM PMID:19224199
RT Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550.
RA Mennenga B, Kay CW, Gorisch H
RL Arch Microbiol. 2009 Apr;191(4):361-7. doi: 10.1007/s00203-009-0460-4. |
| Genome Property | GenProp0170: coenzyme PQQ biosynthesis (HMM) |
| | GenProp1101: quinoprotein cytochrome relay system (HMM) |
