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InterPro: IPR008397 Alginate lyase

Protein matches Help

UniProtKB

Matches:

56 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

IPR008397 Alginate_lyase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:1.50.10.110	Alginate_lyase	49
Pfam	PF05426	Alginate_lyase	46
Signatures in BioMart

InterPro Relationships Help

Contains

IPR008929 Chondroitin AC/alginate lyase

GO Term annotation Help

Process

GO:0042122 alginic acid catabolic process

Function

GO:0045135 poly(beta-D-mannuronate) lyase activity

Component

GO:0042597 periplasmic space

InterPro annotation

Entry Details in BioMart

Abstract

This family contains several bacterial alginate lyase proteins. Alginate is a family of 1-4-linked copolymers of beta -D-mannuronic acid (M) and alpha -L-guluronic acid (G). It is produced by brown algae and by some bacteria belonging to the genera Azotobacter and Pseudomonas. Alginate lyases catalyse the depolymerisation of alginates by beta -elimination, generating a molecule containing 4-deoxy-L-erythro-hex-4-enepyranosyluronate at the nonreducing end [1].

Structural links Help

PDB - click here

SCOP: a.102.3.1

CATH: 1.50.10.110

Database links Help

Enzyme: EC:4.2.2.3

PANDIT: PF05426

Blocks: IPB008397

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR008397

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A5W8V4 Alginate lyase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008929	Chondroitin AC/alginate lyase
IPR008397	Alginate lyase

Publications Open in usermanual
1.	Ertesvag H, Erlien F, Skjak-Braek G, Rehm BH, Valla S. Biochemical properties and substrate specificities of a recombinantly produced Azotobacter vinelandii alginate lyase. J. Bacteriol. 180 3779-84 1998 [PubMed: 9683471] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=9683471&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Yoon HJ, Mikami B, Hashimoto W, Murata K. Crystal structure of alginate lyase A1-III from Sphingomonas species A1 at 1.78 A resolution. J. Mol. Biol. 290 1999 505-14 [PubMed: 10390348] http://dx.doi.org/10.1006/jmbi.1999.2883
	Yoon HJ, Hashimoto W, Miyake O, Murata K, Mikami B. Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 A resolution. J. Mol. Biol. 307 2001 9-16 [PubMed: 11243798] http://dx.doi.org/10.1006/jmbi.2000.4509

InterPro 23.1