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InterPro: IPR020082 S-adenosyl-L-homocysteine hydrolase, conserved site

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UniProtKB

Matches:

1133 proteins

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

Accession

IPR020082 S-Ado-L-homoCys_hydrolase_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00738	ADOHCYASE_1	1037
PROSITE pattern	PS00739	ADOHCYASE_2	1087
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000043 S-adenosyl-L-homocysteine hydrolase
IPR015878 S-adenosyl-L-homocysteine hydrolase, NAD binding
IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0006730 one-carbon metabolic process

Function

GO:0004013 adenosylhomocysteinase activity

InterPro annotation

Entry Details in BioMart

Abstract

S-adenosyl-L-homocysteine hydrolase (EC:3.3.1.1) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine. AdoHcyase is an ubiquitous enzyme which binds and requires NAD⁺ as a cofactor. AdoHcyase is a highly conserved protein [1] of about 430 to 470 amino acids. The family contains a glycine-rich region in the central part of AdoHcyase, which is thought to be involved in NAD-binding.

This entry represents two highly conserved regions. The first pattern is located in the N-terminal section; the second is derived from a glycine-rich region in the central part of S-adenosyl-L-homocysteine hydrolase, a region thought to be involved in NAD-binding.

Structural links Help

PDB - click here

SCOP: c.2.1.4 , c.23.12.3

CATH: 3.40.50.1480 , 3.40.50.720

Database links Help

Enzyme: EC:3.3.1.1

CluSTr: ALLvsALL:2690:110.5

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR020082

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P23526 Adenosylhomocysteinase

P27604 Adenosylhomocysteinase

P39954 Adenosylhomocysteinase

P50245 Putative adenosylhomocysteinase 2

P50247 Adenosylhomocysteinase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020082	S-adenosyl-L-homocysteine hydrolase, conserved site
IPR016040	NAD(P)-binding domain
IPR000043	S-adenosyl-L-homocysteine hydrolase
IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Sganga MW, Aksamit RR, Cantoni GL, Bauer CE. Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus. Proc. Natl. Acad. Sci. U.S.A. 89 6328-32 1992 [PubMed: 1631127] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=1631127

Additional Reading Open in usermanual
	Yamada T, Komoto J, Lou K, Ueki A, Hua DH, Sugiyama K, Takata Y, Ogawa H, Takusagawa F. Structure and function of eritadenine and its 3-deaza analogues: potent inhibitors of S-adenosylhomocysteine hydrolase and hypocholesterolemic agents. Biochem. Pharmacol. 73 2007 981-9 [PubMed: 17214973] http://dx.doi.org/10.1016/j.bcp.2006.12.014
	Tanaka N, Nakanishi M, Kusakabe Y, Shiraiwa K, Yabe S, Ito Y, Kitade Y, Nakamura KT. Crystal structure of S-adenosyl-L-homocysteine hydrolase from the human malaria parasite Plasmodium falciparum. J. Mol. Biol. 343 2004 1007-17 [PubMed: 15476817] http://dx.doi.org/10.1016/j.jmb.2004.08.104
	Yang X, Hu Y, Yin DH, Turner MA, Wang M, Borchardt RT, Howell PL, Kuczera K, Schowen RL. Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions. Biochemistry 42 2003 1900-9 [PubMed: 12590576] http://dx.doi.org/10.1021/bi0262350
	Takata Y, Yamada T, Huang Y, Komoto J, Gomi T, Ogawa H, Fujioka M, Takusagawa F. Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190. J. Biol. Chem. 277 2002 22670-6 [PubMed: 11927587] http://dx.doi.org/10.1074/jbc.M201116200
	Yamada T, Takata Y, Komoto J, Gomi T, Ogawa H, Fujioka M, Takusagawa F. Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Aspl89. Int. J. Biochem. Cell Biol. 37 2005 2417-35 [PubMed: 16061414] http://dx.doi.org/10.1016/j.biocel.2005.06.009

InterPro 23.1