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InterPro: IPR010049 MTA/SAH nucleosidase

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UniProtKB

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1148 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
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Accession List
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Accession

IPR010049 MTA_SAH_Nsdase

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01704	MTA/SAH-Nsdase	1148
Signatures in BioMart

InterPro Relationships Help

Parent

IPR018017 Nucleoside phosphorylase, family 1

GO Term annotation Help

Process

GO:0009164 nucleoside catabolic process
GO:0019509 methionine salvage

Function

GO:0008782 adenosylhomocysteine nucleosidase activity
GO:0008930 methylthioadenosine nucleosidase activity

InterPro annotation

Entry Details in BioMart

Abstract

This entry represents the enzyme 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase which acts on its two substrates at the same active site. This enzyme is involved in the recycling of the components of S-adenosylmethionine after it has donated one of its two non-ribose sulphur ligands to an acceptor. In the case of 5'-methylthioadenosine this represents the first step of the methionine salvage pathway in bacteria [1, 2,]. This enzyme is widely distributed in bacteria.

Structural links Help

PDB - click here

SCOP: c.56.2.1

CATH: 3.40.50.1580

Database links Help

Enzyme: EC:3.2.2.9

CluSTr: ALLvsALL:39278:40

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR010049

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0AF12 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010049	MTA/SAH nucleosidase
IPR018017	Nucleoside phosphorylase, family 1
IPR000845	Nucleoside phosphorylase
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Sekowska A, Danchin A. Identification of yrrU as the methylthioadenosine nucleosidase gene in Bacillus subtilis. DNA Res. 6 255-64 1999 [PubMed: 10574451] http://dx.doi.org/10.1093/dnares/6.5.255
2.	Lee JE, Cornell KA, Riscoe MK, Howell PL. Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases. Structure 9 941-53 2001 [PubMed: 11591349] http://dx.doi.org/10.1016/S0969-2126(01)00656-6

Additional Reading Open in usermanual
	Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL. Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis. J. Mol. Biol. 352 2005 559-74 [PubMed: 16109423] http://dx.doi.org/10.1016/j.jmb.2005.07.027
	Lee JE, Singh V, Evans GB, Tyler PC, Furneaux RH, Cornell KA, Riscoe MK, Schramm VL, Howell PL. Structural rationale for the affinity of pico- and femtomolar transition state analogues of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase. J. Biol. Chem. 280 2005 18274-82 [PubMed: 15746096] http://dx.doi.org/10.1074/jbc.M414471200
	Sekowska A, Danchin A. The methionine salvage pathway in Bacillus subtilis. BMC Microbiol. 2 2002 8 [PubMed: 12022921] http://dx.doi.org/10.1186/1471-2180-2-8
	Lee JE, Cornell KA, Riscoe MK, Howell PL. Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis. J. Biol. Chem. 278 2003 8761-70 [PubMed: 12496243] http://dx.doi.org/10.1074/jbc.M210836200

InterPro 23.1