| Accession | TIGR03872 |
| Name | cytochrome_MoxG |
| Function | cytochrome c(L), periplasmic |
| Gene Symbol | moxG |
| Trusted Cutoff | 147.80 |
| Domain Trusted Cutoff | 147.80 |
| Noise Cutoff | 61.05 |
| Domain Noise Cutoff | 61.05 |
| Isology Type | equivalog |
| HMM Length | 133 |
| Mainrole Category | Energy metabolism |
| Subrole Category | Electron transport |
| Gene Ontology Term | GO:0009055: electron carrier activity molecular_function |
| | GO:0042597: periplasmic space cellular_component |
| | GO:0046170: methanol catabolic process biological_process |
| | GO:0070069: cytochrome complex cellular_component |
| Author | Haft DH |
| Entry Date | Oct 16 2009 10:53AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This model describes a periplasmic c-type cytochrome that serves as the primary electron acceptor for the quinoprotein methanol dehydrogenase, a PQQ enzyme. The member from Paracoccus denitrificans is also characterized as an electron acceptor for methylamine dehydrogenase, a tryptophan tryptophylquinone enzyme. This protein is called cytochrome c(L) in methylotrophic bacteria such Methylobacterium extorquens, but c551i in Paracoccus denitrificans. |
| References | RN [1]
RM PMID:16414073
RT The 1.6A X-ray structure of the unusual c-type cytochrome, cytochrome cL, from the methylotrophic bacterium Methylobacterium extorquens.
RA Williams P, Coates L, Mohammed F, Gill R, Erskine P, Bourgeois D, Wood SP, Anthony C, Cooper JB
RL J Mol Biol. 2006 Mar 17;357(1):151-62. Epub 2006 Jan 5. |
