Species | Cellulomonas massiliensis | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas massiliensis | |||||||||||
CAZyme ID | MGYG000001416_00517 | |||||||||||
CAZy Family | GH64 | |||||||||||
CAZyme Description | Glucan endo-1,3-beta-glucosidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 557731; End: 559356 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH64 | 36 | 394 | 5.1e-119 | 0.9918256130790191 |
CBM13 | 422 | 540 | 6.2e-27 | 0.6436170212765957 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd09216 | GH64-LPHase-like | 3.22e-158 | 38 | 394 | 1 | 352 | glycoside hydrolase family 64: laminaripentaose-producing, beta-1,3-glucanase (LPHase)-like. This subfamily is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain. |
pfam16483 | Glyco_hydro_64 | 1.21e-123 | 36 | 394 | 1 | 370 | Beta-1,3-glucanase. Family 64 glycoside hydrolases have beta-1,3-glucanase activity. |
cd09214 | GH64-like | 2.43e-68 | 38 | 395 | 1 | 319 | glycosyl hydrolase 64 family. This family is represented by the laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis and related bacterial and ascomycete proteins. LPHase is a member of glycoside hydrolase family 64 (GH64), it is an inverting enzyme involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. LPHase is a two-domain crescent fold structure: one domain is composed of 10 beta-strands, eight coming from the N-terminus of the protein and two from the C-terminal region, and the protein has a second inserted domain; this cd includes both domains. This protein has an electronegative, substrate-binding cleft, and conserved Glu and Asp residues involved in the cleavage of the beta-1,3-glucan, laminarin, a plant and fungal cell wall component. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. Also included in this family is GluB , the beta-1,3-glucanase B from Lysobacter enzymogenes Strain N4-7. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. In the Cellulosimicrobium cellulans, glucan endo-1,3-beta-glucosidase, they are positioned N-terminal of a RICIN, carbohydrate-binding domain, and in the Salinispora tropica CNB-440, coagulation factor 5/8 C-terminal domain (FA58C) protein, they are positioned C-terminal of two FA58C domains which are proposed to function as cell surface-attached, carbohydrate-binding domain. This FA58C-containing protein has an internal peptide deletion (of approx. 44 residues) in the LPHase domain II. |
cd09220 | GH64-GluB-like | 3.05e-68 | 38 | 387 | 1 | 361 | glycoside hydrolase family 64: beta-1,3-glucanase B (GluB)-like. This subfamily is represented by GluB, beta-1,3-glucanase B , from Lysobacter enzymogenes Strain N4-7 and related bacterial and ascomycete proteins. GluB is a member of the glycoside hydrolase family 64 (GH64) involved in the cleavage of long-chain polysaccharide beta-1,3-glucans, into specific pentasaccharide oligomers. Among bacteria, many beta-1,3-glucanases are implicated in fungal cell wall degradation. GluB possesses the conserved Glu and Asp residues required to cleave substrate beta-1,3-glucans. Recombinant GluB demonstrated higher relative activity toward the branched-chain beta-1,3 glucan substrate zymosan A than toward linear beta-1,3 glucan substrates. Based on the structure of laminaripentaose-producing, beta-1,3-glucanase (LPHase) of Streptomyces matensis, which belongs to the same family as GluB but to a different subfamily, this cd is a two-domain model. Sometimes these two domains are found associated with other domains such as in the Catenulispora acidiphila DSM 44928 carbohydrate binding family 6 protein in which they are positioned N-terminal of a carbohydrate binding module, family 6 (CBM_6) domain. |
NF035929 | lectin_1 | 9.91e-36 | 417 | 540 | 711 | 836 | lectin. Lectins are important adhesin proteins, which bind carbohydrate structures on host cell surface. The carbohydrate specificity of diverse lectins to a large extent dictates bacteria tissue tropism by mediating specific attachment to unique host sites expressing the corresponding carbohydrate receptor. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QHT57069.1 | 3.44e-237 | 11 | 459 | 11 | 454 |
VEH36237.1 | 2.45e-235 | 1 | 459 | 1 | 456 |
AEE47443.1 | 2.45e-235 | 1 | 459 | 1 | 456 |
QVI65414.1 | 1.27e-233 | 11 | 459 | 9 | 450 |
QCB92217.1 | 1.16e-212 | 1 | 457 | 1 | 449 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3GD0_A | 8.44e-126 | 35 | 398 | 4 | 367 | ChainA, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis],3GD9_A Chain A, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis] |
5H4E_A | 1.07e-30 | 106 | 390 | 89 | 369 | Crystalstructure of a beta-1,3-glucanase domain (GH64) from Clostridium beijerinckii [Clostridium beijerinckii NCIMB 8052] |
5H9X_A | 2.22e-13 | 27 | 388 | 124 | 436 | Crystalstructure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii] |
5H9Y_A | 1.22e-12 | 27 | 388 | 124 | 436 | Crystalstructure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose. [Paenibacillus barengoltzii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q59146 | 3.30e-105 | 12 | 455 | 15 | 461 | Glucan endo-1,3-beta-glucosidase OS=Arthrobacter sp. (strain YCWD3) OX=79671 GN=glcI PE=3 SV=1 |
P22222 | 1.84e-104 | 12 | 455 | 15 | 461 | Glucan endo-1,3-beta-glucosidase OS=Cellulosimicrobium cellulans OX=1710 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.000499 | 0.998447 | 0.000203 | 0.000379 | 0.000233 | 0.000186 |
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