Accession | TIGR03313 |
Name | Se_sel_red_Mo |
Function | probable selenate reductase, molybdenum-binding subunit |
Trusted Cutoff | 1101.90 |
Domain Trusted Cutoff | 1101.90 |
Noise Cutoff | 526.50 |
Domain Noise Cutoff | 526.50 |
Isology Type | hypoth_equivalog |
HMM Length | 951 |
Author | Haft DH |
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. |
References | RN [1]
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.
RN [2]
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) |