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InterPro: IPR002509 Polysaccharide deacetylase

Protein matches Help

UniProtKB

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5993 proteins

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

Accession

IPR002509 Polysac_deacetylase

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.20.20.370	Polysac_deacetylase	5209
Pfam	PF01522	Polysacc_deac_1	5926
Signatures in BioMart

InterPro Relationships Help

Parent

IPR011330 Glycoside hydrolase/deacetylase, beta/alpha-barrel

Children

IPR017625 Putative urate catabolism protein

Found in

IPR014132 Sporulation polysaccharide deacetylase, PdaB
IPR014228 Sporulation protein, polysaccharide deacetylase, YlxY
IPR014235 Delta-lactam-biosynthetic de-N-acetylase
IPR014344 PEP-CTERM locus, polysaccharide deactylase
IPR017219 Peptidoglycan GlcNAc deacetylase

GO Term annotation Help

Process

GO:0005975 carbohydrate metabolic process

Function

GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds

InterPro annotation

Entry Details in BioMart

Abstract

This domain is found in polysaccharide deacetylase. This family of polysaccharide deacetylases includes NodB (nodulation protein B from Rhizobium) which is a chitooligosaccharide deacetylase [1]. It also includes chitin deacetylase from yeast [2], and endoxylanases which hydrolyses glucosidic bonds in xylan [3].

Structural links Help

PDB - click here

SCOP: c.6.2.3 , c.6.2.6

CATH: 3.20.20.370

Database links Help

Enzyme: EC:3

PANDIT: PF01522

Blocks: IPB002509

Pfam Clan: CL0158.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002509

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O34928 Probable polysaccharide deacetylase pdaA

Q06702 Chitin deacetylase 1

Q59006 Putative alpha-amylase

Q8SU65 Polysaccharide deacetylase domain-containing protein ECU11_0510

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004300	Glycoside hydrolase, family 57, core
IPR002509	Polysaccharide deacetylase
IPR011330	Glycoside hydrolase/deacetylase, beta/alpha-barrel
IPR014235	Delta-lactam-biosynthetic de-N-acetylase
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Freiberg C, Fellay R, Bairoch A, Broughton WJ, Rosenthal A, Perret X. Molecular basis of symbiosis between Rhizobium and legumes. Nature 387 394-401 1997 [PubMed: 9163424] http://dx.doi.org/10.1038/387394a0
2.	Mishra C, Semino CE, McCreath KJ, de la Vega H, Jones BJ, Specht CA, Robbins PW. Cloning and expression of two chitin deacetylase genes of Saccharomyces cerevisiae. Yeast 13 327-36 1997 [PubMed: 9133736] http://dx.doi.org/10.1002/(SICI)1097-0061(19970330)13:4<327::AID-YEA96>3.0.CO;2-T
3.	Millward-Sadler SJ, Poole DM, Henrissat B, Hazlewood GP, Clarke JH, Gilbert HJ. Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases. Mol. Microbiol. 11 375-82 1994 [PubMed: 8170399] http://dx.doi.org/10.1111/j.1365-2958.1994.tb00317.x

Additional Reading Open in usermanual
	Blair DE, Hekmat O, Schuttelkopf AW, Shrestha B, Tokuyasu K, Withers SG, van Aalten DM. Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum. Biochemistry 45 2006 9416-26 [PubMed: 16878976] http://dx.doi.org/10.1021/bi0606694
	Oberbarnscheidt L, Taylor EJ, Davies GJ, Gloster TM. Structure of a carbohydrate esterase from Bacillus anthracis. Proteins 66 2007 250-2 [PubMed: 17063474] http://dx.doi.org/10.1002/prot.21217
	Blair DE, Schuttelkopf AW, MacRae JI, van Aalten DM. Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor. Proc. Natl. Acad. Sci. U.S.A. 102 2005 15429-34 [PubMed: 16221761] http://dx.doi.org/10.1073/pnas.0504339102
	Blair DE, van Aalten DM. Structures of Bacillus subtilis PdaA, a family 4 carbohydrate esterase, and a complex with N-acetyl-glucosamine. FEBS Lett. 570 2004 13-9 [PubMed: 15251431] http://dx.doi.org/10.1016/j.febslet.2004.06.013
	Taylor EJ, Gloster TM, Turkenburg JP, Vincent F, Brzozowski AM, Dupont C, Shareck F, Centeno MS, Prates JA, Puchart V, Ferreira LM, Fontes CM, Biely P, Davies GJ. Structure and activity of two metal ion-dependent acetylxylan esterases involved in plant cell wall degradation reveals a close similarity to peptidoglycan deacetylases. J. Biol. Chem. 281 2006 10968-75 [PubMed: 16431911] http://dx.doi.org/10.1074/jbc.M513066200

InterPro 23.1