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CAZyme Information: MGYG000000208_01693

You are here: Home > Sequence: MGYG000000208_01693

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Eubacterium_G ventriosum
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_G; Eubacterium_G ventriosum
CAZyme ID MGYG000000208_01693
CAZy Family GH64
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
615 67882.45 4.7052
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000208 2760783 Isolate China Asia
Gene Location Start: 135448;  End: 137295  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000208_01693.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH64 262 613 1.9e-96 0.9863760217983651

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09214 GH64-like 1.02e-115 262 613 1 318
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.
pfam16483 Glyco_hydro_64 4.51e-89 264 613 5 370
Beta-1,3-glucanase. Family 64 glycoside hydrolases have beta-1,3-glucanase activity.
cd09216 GH64-LPHase-like 1.54e-53 270 613 6 352
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.
cd09220 GH64-GluB-like 7.58e-31 334 611 71 366
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.
pfam04886 PT 1.03e-05 104 140 2 36
PT repeat. This short repeat is composed on the tetrapeptide XPTX. This repeat is found in a variety of proteins, however it is not clear if these repeats are homologous to each other. The alignment represents nine copies of this repeat.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AWI66982.1 5.94e-137 238 615 89 477
CUU48451.1 8.06e-96 256 615 217 589
AJG99223.1 2.23e-95 256 615 217 589
ABR34974.1 1.71e-94 256 615 217 589
QUF72014.1 1.71e-94 256 615 217 589

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5H4E_A 1.24e-98 256 615 3 375
Crystalstructure of a beta-1,3-glucanase domain (GH64) from Clostridium beijerinckii [Clostridium beijerinckii NCIMB 8052]
5H9X_A 3.97e-68 262 615 137 444
Crystalstructure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5H9Y_A 2.95e-67 262 615 137 444
Crystalstructure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose. [Paenibacillus barengoltzii]
3GD0_A 8.70e-29 338 601 79 351
ChainA, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis],3GD9_A Chain A, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q59146 1.67e-19 338 613 111 394
Glucan endo-1,3-beta-glucosidase OS=Arthrobacter sp. (strain YCWD3) OX=79671 GN=glcI PE=3 SV=1
P22222 2.95e-19 338 613 111 394
Glucan endo-1,3-beta-glucosidase OS=Cellulosimicrobium cellulans OX=1710 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.995429 0.004572 0.000012 0.000006 0.000003 0.000006

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000208_01693.