|Function||NDMA-dependent methanol dehydrogenase|
|Domain Trusted Cutoff||625.00|
|Domain Noise Cutoff||400.00|
|Entry Date||Jan 16 2012 9:35AM|
|Last Modified||Apr 28 2014 12:11PM|
|Comment||Members of this family belong to the iron-dependent alcohol dehydrogenase family (see PF00465). The NADP(H) cofactor is bound too tightly for exchange (although non-convalently), so enzymatic activity depends on a second substrate or electron carrier. The radical SAM-modified natural product mycofactocin is proposed to fill this role. In Rhodococcus erythropolis N9T-4, a role was shown for this protein in CO2 fixation during extreme oligotrophic (or possibly chemoautotrophic) growth.|
RT Electron microscopic analysis and structural characterization of novel NADP(H)-containing methanol: N,N'-dimethyl-4-nitrosoaniline oxidoreductases from the gram-positive methylotrophic bacteria Amycolatopsis methanolica and Mycobacterium gastri MB19.
RA Bystrykh LV, Vonck J, van Bruggen EF, van Beeumen J, Samyn B, Govorukhina NI, Arfman N, Duine JA, Dijkhuizen L
RL J Bacteriol. 1993 Mar;175(6):1814-22.
RT Bioinformatic evidence for a widely distributed, ribosomally produced electron carrier precursor, its maturation proteins, and its nicotinoprotein redox partners.
RA Haft DH
RL BMC Genomics. 2011 Jan 11;12:21.
RT An extremely oligotrophic bacterium, Rhodococcus erythropolis N9T-4, isolated from crude oil.
RA Ohhata N, Yoshida N, Egami H, Katsuragi T, Tani Y, Takagi H
RL J Bacteriol. 2007 Oct;189(19):6824-31.|
|Genome Property||GenProp0917: mycofactocin system (HMM)|
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