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InterPro: IPR006034 Asparaginase/glutaminase

Protein matches Help

UniProtKB

Matches:

2040 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

IPR006034 Asparaginase/glutaminase

Secondary

IPR000267

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00710	Asparaginase	1914
PRINTS	PR00139	ASNGLNASE	1857
PANTHER	PTHR11707	Asp/Glutamnse	2020
SMART	SM00870	Asparaginase	1849
SuperFamily	SSF53774	Asp/Glutamnse	1921
Signatures in BioMart

InterPro Relationships Help

Children

IPR004550 L-asparaginase, type II
IPR006033 L-asparaginase, type I
IPR011878 Glutamyl-tRNA(Gln) amidotransferase, subunit E

Contains

IPR020827 Asparaginase/glutaminase, conserved site

GO Term annotation Help

Process

GO:0006520 cellular amino acid metabolic process

InterPro annotation

Entry Details in BioMart

Abstract

Asparaginase, which is found in various plant, animal and bacterial cells, catalyses the deamination of asparagine to yield aspartic acid and an ammonium ion, resulting in a depletion of free circulatory asparagine in plasma [1]. The enzyme is effective in the treatment of human malignant lymphomas, which have a diminished capacity to produce asparagine synthetase: in order to survive, such cells absorb asparagine from blood plasma [2, 3] - if Asn levels have been depleted by injection of asparaginase, the lymphoma cells die. Glutaminase, a similar enzyme, catalyses the deaminination of glutamine to glutamic acid and an ammonium ion [2]. Both enzymes are homotetramers [1]: two threonine residues in the N-terminal half of the proteins are involved in the catalytic activity.

Structural links Help

PDB - click here

SCOP: c.88.1.1

CATH: 3.40.50.1170 , 3.40.50.40

Database links Help

PDBe-motif: PS00144 , PS00917

PROSITE doc: PDOC00132

PANDIT: PF00710

Blocks: IPB006034

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006034

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A0JNU3 60 kDa lysophospholipase

P00805 L-asparaginase 2

P11163 L-asparaginase 2

Q5UPV5 Putative ankyrin repeat protein L279

Q86U10 60 kDa lysophospholipase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR020827	Asparaginase/glutaminase, conserved site
IPR006034	Asparaginase/glutaminase
IPR006033	L-asparaginase, type I
IPR002110	Ankyrin repeat
IPR020683	Ankyrin repeat-containing domain
IPR004550	L-asparaginase, type II
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Minton NP, Bullman HM, Scawen MD, Atkinson T, Gilbert HJ. Nucleotide sequence of the Erwinia chrysanthemi NCPPB 1066 L-asparaginase gene. Gene 46 25-35 1986 [PubMed: 3026924] http://dx.doi.org/10.1016/0378-1119(86)90163-0
2.	Jennings MP, Beacham IR. Analysis of the Escherichia coli gene encoding L-asparaginase II, ansB, and its regulation by cyclic AMP receptor and FNR proteins. J. Bacteriol. 172 1491-8 1990 [PubMed: 2407723] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=2407723&action=stream&blobtype=pdf
3.	Tanaka S, Robinson EA, Appella E, Miller M, Ammon HL, Roberts J, Weber IT, Wlodawer A. Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi. J. Biol. Chem. 263 8583-91 1988 [PubMed: 3379033] http://intl.jbc.org/cgi/reprint/263/18/8583.pdf

Additional Reading Open in usermanual
	Lubkowski J, Dauter M, Aghaiypour K, Wlodawer A, Dauter Z. Atomic resolution structure of Erwinia chrysanthemi L-asparaginase. Acta Crystallogr. D Biol. Crystallogr. 59 2003 84-92 [PubMed: 12499544]
	Jaskolski M, Kozak M, Lubkowski J, Palm G, Wlodawer A. Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups. Acta Crystallogr. D Biol. Crystallogr. 57 2001 369-77 [PubMed: 11223513] http://dx.doi.org/10.1107/S0907444900020175
	Oshikane H, Sheppard K, Fukai S, Nakamura Y, Ishitani R, Numata T, Sherrer RL, Feng L, Schmitt E, Panvert M, Blanquet S, Mechulam Y, Soll D, Nureki O. Structural basis of RNA-dependent recruitment of glutamine to the genetic code. Science 312 2006 1950-4 [PubMed: 16809540] http://dx.doi.org/10.1126/science.1128470
	Schmitt E, Panvert M, Blanquet S, Mechulam Y. Structural basis for tRNA-dependent amidotransferase function. Structure 13 2005 1421-33 [PubMed: 16216574] http://dx.doi.org/10.1016/j.str.2005.06.016
	Sanches M, Barbosa JA, de Oliveira RT, Abrahao Neto J, Polikarpov I. Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups. Acta Crystallogr. D Biol. Crystallogr. 59 2003 416-22 [PubMed: 12595697] http://dx.doi.org/10.1107/S0907444902021200

InterPro 23.1