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InterPro: IPR006650 Adenosine/AMP deaminase active site

Protein matches Help

UniProtKB

Matches:

429 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

IPR006650 A/AMP_deam_AS

Secondary

IPR001365

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00485	A_DEAMINASE	429
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001365 Adenosine/AMP deaminase
IPR006330 Adenosine deaminase

GO Term annotation Help

Process

GO:0009168 purine ribonucleoside monophosphate biosynthetic process

Function

GO:0019239 deaminase activity

InterPro annotation

Entry Details in BioMart

Abstract

Adenosine deaminase (EC:3.5.4.4) catalyzes the hydrolytic deamination of adenosine into inosine and AMP deaminase (EC:3.5.4.6) catalyzes the hydrolytic deamination of AMP into IMP. It has been shown [1] that these two enzymes share three regions of sequence similarities; these regions are centred on residues which are proposed to play an important role in the catalytic mechanism of these two enzymes. This entry presents one of these regions, it contains two conserved aspartic acid residues that are potential active site residues.

Structural links Help

PDB - click here

SCOP: c.1.9.1

CATH: 3.20.20.140

Database links Help

PDBe-motif: PS00485

Enzyme: EC:3.5.4.4

PROSITE doc: PDOC00419

Blocks: IPB006650

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006650

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O80452 AMP deaminase

P00813 Adenosine deaminase

P03958 Adenosine deaminase

P15274 AMP deaminase

Q84NP7 Probable AMP deaminase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR006330	Adenosine deaminase
IPR016297	AMP deaminase, metazoa
IPR006329	AMP deaminase
IPR006650	Adenosine/AMP deaminase active site
IPR001365	Adenosine/AMP deaminase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Chang ZY, Nygaard P, Chinault AC, Kellems RE. Deduced amino acid sequence of Escherichia coli adenosine deaminase reveals evolutionarily conserved amino acid residues: implications for catalytic function. Biochemistry 30 2273-80 1991 [PubMed: 1998686] http://dx.doi.org/10.1021/bi00222a033

Additional Reading Open in usermanual
	Weihofen WA, Liu J, Reutter W, Saenger W, Fan H. Crystal structures of HIV-1 Tat-derived nonapeptides Tat-(1-9) and Trp2-Tat-(1-9) bound to the active site of dipeptidyl-peptidase IV (CD26). J. Biol. Chem. 280 2005 14911-7 [PubMed: 15695814] http://dx.doi.org/10.1074/jbc.M413400200
	Han BW, Bingman CA, Mahnke DK, Bannen RM, Bednarek SY, Sabina RL, Phillips GN Jr. Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1). J. Biol. Chem. 281 2006 14939-47 [PubMed: 16543243] http://dx.doi.org/10.1074/jbc.M513009200
	Vedadi M, Lew J, Artz J, Amani M, Zhao Y, Dong A, Wasney GA, Gao M, Hills T, Brokx S, Qiu W, Sharma S, Diassiti A, Alam Z, Melone M, Mulichak A, Wernimont A, Bray J, Loppnau P, Plotnikova O, Newberry K, Sundararajan E, Houston S, Walker J, Tempel W, Bochkarev A, Kozieradzki I, Edwards A, Arrowsmith C, Roos D, Kain K, Hui R. Genome-scale protein expression and structural biology of Plasmodium falciparum and related Apicomplexan organisms. Mol. Biochem. Parasitol. 151 2007 100-10 [PubMed: 17125854] http://dx.doi.org/10.1016/j.molbiopara.2006.10.011
	Kinoshita T, Tada T, Nakanishi I. Conformational change of adenosine deaminase during ligand-exchange in a crystal. Biochem. Biophys. Res. Commun. 373 2008 53-7 [PubMed: 18549808] http://dx.doi.org/10.1016/j.bbrc.2008.05.180
	Han BW, Bingman CA, Mahnke DK, Sabina RL, Phillips GN Jr. Crystallization and preliminary X-ray crystallographic analysis of adenosine 5'-monophosphate deaminase (AMPD) from Arabidopsis thaliana in complex with coformycin 5'-phosphate. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 2005 740-2 [PubMed: 16511144]

InterPro 23.1