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InterPro: IPR015878 S-adenosyl-L-homocysteine hydrolase, NAD binding

Protein matches Help

UniProtKB

Matches:

1217 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

IPR015878 Ado_hCys_hydrolase_NAD-bd

Secondary

IPR000043

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00670	AdoHcyase_NAD	1217
Signatures in BioMart

InterPro Relationships Help

Parent

IPR016040 NAD(P)-binding domain

Found in

IPR000043 S-adenosyl-L-homocysteine hydrolase

Contains

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

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.

This entry represents the glycine-rich region in the central part of AdoHcyase, which is thought to be involved in NAD-binding.

Structural links Help

PDB - click here

SCOP: c.2.1.4

CATH: 3.40.50.1480 , 3.40.50.720

Database links Help

Enzyme: EC:3.3.1.1

PANDIT: PF00670

CluSTr: ALLvsALL:2690:110.5

Pfam Clan: CL0063.21

AC	CL0063.21
ID	NADP_Rossmann
DE	FAD/NAD(P)-binding Rossmann fold Superfamily
PF00044	IPR020828	Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain
PF00056	IPR001236	Lactate/malate dehydrogenase
PF00070	IPR001327	Pyridine nucleotide-disulphide oxidoreductase, NAD-binding region
PF00106	IPR002198	Short-chain dehydrogenase/reductase SDR
PF00107	IPR013149	Alcohol dehydrogenase, zinc-binding
PF00208	IPR006096	Glutamate/phenylalanine/leucine/valine dehydrogenase, C-terminal
PF00479	IPR001282	Glucose-6-phosphate dehydrogenase
PF00670	IPR015878	S-adenosyl-L-homocysteine hydrolase, NAD binding
PF00732	IPR000172	Glucose-methanol-choline oxidoreductase, N-terminal
PF00743	IPR000960	Flavin-containing monooxygenase FMO
PF00890	IPR003953	Fumarate reductase/succinate dehydrogenase flavoprotein, N-terminal
PF00899	IPR000594	UBA/THIF-type NAD/FAD binding fold
PF00996	IPR018203	GDP dissociation inhibitor
PF01073	IPR002225	3-beta hydroxysteroid dehydrogenase/isomerase
PF01113	IPR000846	Dihydrodipicolinate reductase
PF01118	IPR000534	Semialdehyde dehydrogenase, NAD-binding
PF01134	IPR002218	Glucose-inhibited division protein A-related
PF01210	IPR011128	NAD-dependent glycerol-3-phosphate dehydrogenase, N-terminal
PF01225	IPR000713	Mur ligase, N-terminal
PF01232	IPR013131	Mannitol dehydrogenase, N-terminal
PF01262	IPR007698	Alanine dehydrogenase/PNT, C-terminal
PF01266	IPR006076	FAD dependent oxidoreductase
PF01370	IPR001509	NAD-dependent epimerase/dehydratase
PF01408	IPR000683	Oxidoreductase, N-terminal
PF01488	IPR006151	Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase
PF01494	IPR002938	Monooxygenase, FAD-binding
PF01593	IPR002937	Amine oxidase
PF01946	IPR002922	Thiamine biosynthesis Thi4 protein
PF02153	IPR003099	Prephenate dehydrogenase
PF02254	IPR003148	Regulator of K+ conductance, N-terminal
PF02423	IPR003462	Ornithine cyclodeaminase/mu-crystallin
PF02558	IPR013332	Ketopantoate reductase ApbA/PanE, N-terminal
PF02629	IPR003781	CoA-binding
PF02670	IPR013512	1-deoxy-D-xylulose 5-phosphate reductoisomerase, N-terminal
PF02719	IPR003869	Polysaccharide biosynthesis protein CapD-like
PF02737	IPR006176	3-hydroxyacyl-CoA dehydrogenase, NAD binding
PF02826	IPR006140	D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding
PF02882	IPR020631	Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain
PF03435	IPR005097	Saccharopine dehydrogenase
PF03446	IPR006115	6-phosphogluconate dehydrogenase, NAD-binding
PF03447	IPR005106	Aspartate/homoserine dehydrogenase, NAD-binding
PF03486	IPR004792	HI0933-like protein
PF03721	IPR001732	UDP-glucose/GDP-mannose dehydrogenase, N-terminal
PF03807	IPR004455	NADP oxidoreductase, coenzyme F420-dependent
PF03949	IPR012302	Malic enzyme, NAD-binding
PF04321	IPR005913	dTDP-4-dehydrorhamnose reductase
PF04723	IPR006812	Glycine reductase complex selenoprotein A
PF04820	IPR006905	Tryptophan halogenase
PF05368	IPR008030	NmrA-like
PF05834	IPR008671	Lycopene beta/epsilon cyclase
PF06039	IPR006231	Malate:quinone-oxidoreductase
PF07157	IPR009826	DNA circulation, N-terminal
PF07991	IPR013116	Acetohydroxy acid isomeroreductase, catalytic
PF07992	IPR013027	FAD-dependent pyridine nucleotide-disulphide oxidoreductase
PF07993	IPR013120	Male sterility, NAD-binding
PF07994	IPR002587	Myo-inositol-1-phosphate synthase
PF08491	IPR013698	Squalene epoxidase
PF08659	IPR013968	Polyketide synthase, KR
PF10727	IPR019665	Putative oxidoreductase/dehydrogenase, Rossmann-like domain

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR015878

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