rhamnogalacturonan lyase of the polysaccharide lyase family 11 cleaves glycoside bonds in polygalacturonan and rhamnogalacturonan type-I through a beta-elimination reaction, an important step in degrading plant cell walls
Rhamnogalacturonan lyase of the polysaccharide lyase family 11; The rhamnogalacturonan lyase ...
8-587
0e+00
Rhamnogalacturonan lyase of the polysaccharide lyase family 11; The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
:
Pssm-ID: 199906 [Multi-domain] Cd Length: 564 Bit Score: 1032.21 E-value: 0e+00
Rhamnogalacturonan lyase of the polysaccharide lyase family 11; The rhamnogalacturonan lyase ...
8-587
0e+00
Rhamnogalacturonan lyase of the polysaccharide lyase family 11; The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
Pssm-ID: 199906 [Multi-domain] Cd Length: 564 Bit Score: 1032.21 E-value: 0e+00
Rhamnogalacturonan I lyases beta-sheet domain; This is the beta-sheet domain found in ...
6-91
4.51e-45
Rhamnogalacturonan I lyases beta-sheet domain; This is the beta-sheet domain found in rhamnogalacturonan (RG) lyases, which are responsible for an initial cleavage of the RG type I (RG-I) region of plant cell wall pectin. Polysaccharide lyase family 11 carrying this domain, such as YesW (EC:4.2.2.23) and YesX (EC:4.2.2.24), cleave glycoside bonds between rhamnose and galacturonic acid residues in RG-I through a beta-elimination reaction. Other family members carrying this domain are hemagglutinin A, lysine gingipain (Kgp) and Chitinase C (EC:3.2.1.14).
Pssm-ID: 408170 [Multi-domain] Cd Length: 86 Bit Score: 154.62 E-value: 4.51e-45
Rhamnogalacturonan lyase of the polysaccharide lyase family 11; The rhamnogalacturonan lyase ...
8-587
0e+00
Rhamnogalacturonan lyase of the polysaccharide lyase family 11; The rhamnogalacturonan lyase of the polysaccharide lyase family 11 (RGL11) cleaves glycoside bonds in polygalacturonan as well as RG (rhamnogalacturonan) type-I through a beta-elimination reaction. Functionally characterized members of this family, YesW and YesX from Bacillus subtilis, cleave glycoside bonds between rhamnose and galacturonic acid residues in the RG-I region of plant cell wall pectin. YesW and YesX work synergistically, with YesW cleaving the glycoside bond of the RG chain endolytically, and YesX converting the resultant oligosaccharides through an exotype reaction. This domain is sometimes found in architectures with non-catalytic carbohydrate-binding modules (CBMs). There are two types of RG lyases, which both cleave the alpha-1,4 bonds of the RG-I main chain through a beta-elimination reaction, but belong to two structurally unrelated polysaccharide lyase (PL) families, 4 and 11.
Pssm-ID: 199906 [Multi-domain] Cd Length: 564 Bit Score: 1032.21 E-value: 0e+00
Rhamnogalacturonan I lyases beta-sheet domain; This is the beta-sheet domain found in ...
6-91
4.51e-45
Rhamnogalacturonan I lyases beta-sheet domain; This is the beta-sheet domain found in rhamnogalacturonan (RG) lyases, which are responsible for an initial cleavage of the RG type I (RG-I) region of plant cell wall pectin. Polysaccharide lyase family 11 carrying this domain, such as YesW (EC:4.2.2.23) and YesX (EC:4.2.2.24), cleave glycoside bonds between rhamnose and galacturonic acid residues in RG-I through a beta-elimination reaction. Other family members carrying this domain are hemagglutinin A, lysine gingipain (Kgp) and Chitinase C (EC:3.2.1.14).
Pssm-ID: 408170 [Multi-domain] Cd Length: 86 Bit Score: 154.62 E-value: 4.51e-45
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven ...
331-358
2.67e-03
FG-GAP repeat; This family contains the extracellular repeat that is found in up to seven copies in alpha integrins. This repeat has been predicted to fold into a beta propeller structure. The repeat is called the FG-GAP repeat after two conserved motifs in the repeat. The FG-GAP repeats are found in the N terminus of integrin alpha chains, a region that has been shown to be important for ligand binding. A putative Ca2+ binding motif is found in some of the repeats.
Pssm-ID: 460357 Cd Length: 36 Bit Score: 35.56 E-value: 2.67e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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