|Function||probable selenate reductase, molybdenum-binding subunit|
|Domain Trusted Cutoff||1101.90|
|Domain Noise Cutoff||526.50|
|Entry Date||Feb 15 2007 11:15AM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||Our comparative genomics suggests this protein family to be a subunit of a selenium-dependent molybdenum hydroxylase, although the substrate is not specified. This protein is suggested by Bebien, et al., to be the molybdenum-binding subunit of a molydbopterin-containing selenate reductase. Xi, et al, however, show that mutation of this gene in E. coli conferred sensitivity to adenine, suggesting a defect in purine interconversion. This finding, plus homology of nearby genes in a 23-gene purine catabolism region in E. coli to xanthine dehydrogase subunits suggests xanthine dehydrogenase activity.|
RM PMID: 12480890
RT Involvement of a putative molybdenum enzyme in the reduction of selenate by Escherichia coli.
RA Bebien M, Kirsch J, Mejean V, Vermeglio A
RL Microbiology. 2002 Dec;148(Pt 12):3865-72.
RM PMID: 10986234
RT Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage.
RA Xi H, Schneider BL, Reitzer L
RL J Bacteriol. 2000 Oct;182(19):5332-41.|
|Genome Property||GenProp0726: selenium-dependent molybdenum hydroxylase system (HMM)|
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