SGNH/GDSL hydrolase family protein is a hydrolytic enzyme such as an esterase or lipase; may have multifunctional properties including broad substrate specificity and regiospecificity
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
179-380
6.47e-39
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
:
Pssm-ID: 238869 Cd Length: 169 Bit Score: 137.09 E-value: 6.47e-39
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll ...
69-173
9.22e-39
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.
:
Pssm-ID: 465608 Cd Length: 108 Bit Score: 134.33 E-value: 9.22e-39
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
179-380
6.47e-39
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pssm-ID: 238869 Cd Length: 169 Bit Score: 137.09 E-value: 6.47e-39
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll ...
69-173
9.22e-39
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.
Pssm-ID: 465608 Cd Length: 108 Bit Score: 134.33 E-value: 9.22e-39
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
170-376
2.06e-20
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 87.78 E-value: 2.06e-20
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
179-380
6.47e-39
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Pssm-ID: 238869 Cd Length: 169 Bit Score: 137.09 E-value: 6.47e-39
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll ...
69-173
9.22e-39
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.
Pssm-ID: 465608 Cd Length: 108 Bit Score: 134.33 E-value: 9.22e-39
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
170-376
2.06e-20
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];
Pssm-ID: 442045 [Multi-domain] Cd Length: 191 Bit Score: 87.78 E-value: 2.06e-20
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
180-379
1.42e-11
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
Pssm-ID: 238141 [Multi-domain] Cd Length: 187 Bit Score: 62.81 E-value: 1.42e-11
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
176-380
2.41e-04
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
Pssm-ID: 238874 Cd Length: 191 Bit Score: 41.87 E-value: 2.41e-04
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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