AC   MF_00557;
DC   Protein; auto
TR   HAMAP; MF_00557; -; 1; level=0
XX
Names: Alginate_lyase
XX
ID   ALGL
DE   RecName: Full=Alginate lyase;
DE            EC=4.2.2.3;
DE   AltName: Full=Poly(beta-D-mannuronate) lyase;
case <Feature:Signal>
DE   + Flags: Precursor;
end case
GN   Name=algL;
XX
case defined <Property:Membrane> and <Property:Membrane=2>
CC   -!- FUNCTION: Catalyzes the depolymerization of alginate by cleaving the
CC       beta-1,4 glycosidic bond between two adjacent sugar residues via a
CC       beta-elimination mechanism. May serve to degrade mislocalized alginate
CC       that is trapped in the periplasmic space.
else
CC   -!- FUNCTION: Catalyzes the depolymerization of alginate by cleaving the
CC       beta-1,4 glycosidic bond between two adjacent sugar residues via a
CC       beta-elimination mechanism.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of alginate to give oligosaccharides with
CC         4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing
CC         ends and beta-D-mannuronate at their reducing end.; EC=4.2.2.3;
case defined <Property:Membrane> and <Property:Membrane=2>
CC   -!- SUBCELLULAR LOCATION: Periplasm.
end case
CC   -!- SIMILARITY: Belongs to the polysaccharide lyase 5 family.
XX
DR   Pfam; PF05426; Alginate_lyase; 1; trigger=no
DR   General; Signal; -; 1; trigger=yes
XX
KW   Lyase
case <Feature:Signal>
KW   Signal
end case
case defined <Property:Membrane> and <Property:Membrane=2>
KW   Periplasm
end case
XX
GO   GO:0045135; F:poly(beta-D-mannuronate) lyase activity
GO   GO:0042122; P:alginic acid catabolic process
case defined <Property:Membrane> and <Property:Membrane=2>
GO   GO:0042597; C:periplasmic space
end case
XX
FT   From: ALGL_PSEAE (Q06749)
FT   BINDING         65..66
FT                   /ligand="substrate"
FT   Condition: S-K
FT   BINDING         138..139
FT                   /ligand="substrate"
FT   Condition: H-T
FT   BINDING         256
FT                   /ligand="substrate"
FT   Condition: Y
XX
Size: 367-378;
Related: None;
Template: Q06749; O50660; O52195; Q9L7P2;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.26 2022/05/14
//