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InterPro: IPR013540 Chitinase A N-terminal

Protein matches Help

UniProtKB

Matches:

174 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

IPR013540 ChitinaseA_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF08329	ChitinaseA_N	174
Signatures in BioMart

InterPro Relationships Help

Parent

IPR014756 Immunoglobulin E-set

Contains

IPR013783 Immunoglobulin-like fold

GO Term annotation Help

Function

GO:0004568 chitinase activity

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in a number of bacterial chitinases and similar viral proteins. It is organised into a fibronectin III module domain-like fold, comprising only beta strands. Its function is not known, but it may be involved in interaction with the enzyme substrate, chitin [1, 2]. It is separated by a hinge region from the catalytic domain (IPR001223); this hinge region is probably mobile, allowing the N-terminal domain to have different relative positions in solution [1].

Structural links Help

PDB - click here

SCOP: b.1.18.2 , c.1.8.5

CATH: 2.60.40.10 , 3.20.20.80

Database links Help

Enzyme: EC:3.2.1.14

CluSTr: ALLvsALL:41931:150.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR013540

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O10363 Probable endochitinase

P07254 Chitinase A

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR013781	Glycoside hydrolase, subgroup, catalytic core
IPR013783	Immunoglobulin-like fold
IPR014756	Immunoglobulin E-set
IPR001579	Glycoside hydrolase, chitinase active site
IPR013540	Chitinase A N-terminal
IPR017853	Glycoside hydrolase, catalytic core
IPR011583	Chitinase II
IPR000601	PKD
IPR001223	Glycoside hydrolase, family 18, catalytic domain
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, Wilson KS, Vorgias CE. Crystal structure of a bacterial chitinase at 2.3 A resolution. Structure 2 1169-80 1994 [PubMed: 7704527] http://dx.doi.org/10.1016/S0969-2126(94)00119-7
2.	Perrakis A, Ouzounis C, Wilson KS. Evolution of immunoglobulin-like modules in chitinases: their structural flexibility and functional implications. 2 291-4 1997 [PubMed: 9377712] http://dx.doi.org/10.1016/S1359-0278(97)00040-0

Additional Reading Open in usermanual
	Aronson NN Jr, Halloran BA, Alexeyev MF, Zhou XE, Wang Y, Meehan EJ, Chen L. Mutation of a conserved tryptophan in the chitin-binding cleft of Serratia marcescens chitinase A enhances transglycosylation. Biosci. Biotechnol. Biochem. 70 2006 243-51 [PubMed: 16428843] http://dx.doi.org/10.1271/bbb.70.243
	Papanikolau Y, Prag G, Tavlas G, Vorgias CE, Oppenheim AB, Petratos K. High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Biochemistry 40 2001 11338-43 [PubMed: 11560481] http://dx.doi.org/10.1021/bi010505h
	Papanikolau Y, Tavlas G, Vorgias CE, Petratos K. De novo purification scheme and crystallization conditions yield high-resolution structures of chitinase A and its complex with the inhibitor allosamidin. Acta Crystallogr. D Biol. Crystallogr. 59 2003 400-3 [PubMed: 12554965] http://dx.doi.org/10.1107/S0907444902021923
	Aronson NN Jr, Halloran BA, Alexyev MF, Amable L, Madura JD, Pasupulati L, Worth C, Van Roey P. Family 18 chitinase-oligosaccharide substrate interaction: subsite preference and anomer selectivity of Serratia marcescens chitinase A. Biochem. J. 376 2003 87-95 [PubMed: 12932195] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=12932195

InterPro 23.1