HMM Summary Page: TIGR03313

Functionprobable selenate reductase, molybdenum-binding subunit
Trusted Cutoff1101.90
Domain Trusted Cutoff1101.90
Noise Cutoff526.50
Domain Noise Cutoff526.50
Isology Typehypoth_equivalog
HMM Length951
AuthorHaft DH
Entry DateFeb 15 2007 11:15AM
Last ModifiedFeb 14 2011 3:27PM
CommentOur 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.
ReferencesRN [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 PropertyGenProp0726: selenium-dependent molybdenum hydroxylase system (HMM)