HMM Summary Page: TIGR01705

Functionputative 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Trusted Cutoff152.20
Domain Trusted Cutoff152.20
Noise Cutoff40.85
Domain Noise Cutoff40.85
Isology Typehypoth_equivalog
HMM Length212
AuthorSelengut J
Entry DateSep 26 2002 10:13AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model represents the enzyme 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This clade of sequences is sufficiently distinct from the characterized proteins [1,2] which form the seed of TIGR01704 as to cast some doubt on the accuracy of annotations based on sequence similarity alone. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulfur ligands to an acceptor. In the case of 5'-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria [1,2,3]. This enzyme is widely distributed in bacteria.
ReferencesRN [1] RM PMID: 10574451 RT Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis. RA Sekowska A, Danchin A. RL DNA Res 1999 Oct 29;6(5):255-64 RN [2] RM PMID: 11591349 RT Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. RA Lee JE, Cornell KA, Riscoe MK, Howell PL. RL Structure (Camb) 2001 Oct;9(10):941-53 RN [3] RM PMID: 12022921 RT The methionine salvage pathway in Bacillus subtilis RA Sekowska A, Danchin, A. RL BMC Microbiology 2001; 2:8