CAZyme Information: EPE06073.1

Basic Information

• Species: Ophiostoma piceae
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae
• CAZyme ID: EPE06073.1
• CAZy Family: GH28
• CAZyme Description: Glyco_hydro_64 domain-containing protein [Source:UniProtKB/TrEMBL;Acc:S3CI77]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663		69394.55	5.0476

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346	8884	1262450	0	8884

• Gene Location: location=KE148154:512136-514127(+)

Full Sequence      

MSTLDDCLLKQNNDSILTAPASSSTTSSSNKSSHTPSTASASAAGVTPTSMQIDLRNNTT
SENVYAYVTGLDLNNNSAVFMLQSDGVTAYHPANPAANGTAISEDCAIAVGSPGTVKTVT
IPRLAGARIWFCQDAKLTFLLNMGSSGPGLVEPSVTNKADPNYPLRWDFAEFTFNDYQMF
ANITYVDFISIPTALKLTTTDGSAAQTVKGIPTDGMSTIATLLQDQQKIDCAGWDQLIVQ
ISSASAGTSYLRIVSPDKGAILTEGLFSGYYDDYVNQVWDKYKTETLTINTQNSWGNVTG
KTDSSGNLNFGSAGSVSKPSAGDIFNCSSGAFSANNMNTDELANIGARIAAALNRSTLLT
SASQPNGVTDAADYYQNAITNHYSRIVHSVNLDGRGYTFPYDDVAADGASDQAGAVFSSY
PDKLTVYIGGGDDNGAISSAKARSTPIRLRDMARPGRQLVGGRRQHHRRSVPPPPSDFAD
SVDEKALLQAQDRSTSDSMVDLEKGPTTVSTKGESLYPGAATPSTPDLTARFALLMHQAL
VYMWAAICGLGRSAWALVPRRIAAPVGGFFTRVAESPAMAAVSSSVSSLVSSVIKSAAAS
VVAAMIIRPLVVRAVLTLAVLAVTYAAGVGAGASPALTSAVGAMSGWAESLVGENVTAII
EQQ

Enzyme Prediction     

No EC number prediction in EPE06073.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH64	49	429	6.2e-111	0.9945504087193461

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185759	GH64-GluB-like	1.50e-177	51	429	1	369	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.
406796	Glyco_hydro_64	6.17e-170	49	428	1	370	Beta-1,3-glucanase. Family 64 glycoside hydrolases have beta-1,3-glucanase activity.
185755	GH64-LPHase-like	3.54e-80	57	426	7	350	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.
185753	GH64-like	1.49e-40	51	429	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCD56895.1|GH64	2.51e-135	1	430	1	406
ATZ51080.1|GH64	2.51e-135	1	430	1	406
QKX59108.1|GH64	1.69e-128	44	431	10	385
ACU74083.1|CBM6|GH64	7.69e-128	43	435	30	407
QBZ62949.1|GH64	3.31e-126	1	436	1	422

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GD0_A	3.95e-36	48	404	4	344	Chain A, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis],3GD9_A Chain A, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis]
5H4E_A	1.74e-11	121	404	89	354	Crystal structure of a beta-1,3-glucanase domain (GH64) from Clostridium beijerinckii [Clostridium beijerinckii NCIMB 8052]
5H9X_A	4.57e-08	119	414	211	433	Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
5H9Y_A	2.44e-07	119	414	211	433	Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii complexed with laminarihexaose. [Paenibacillus barengoltzii]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P22222|E13B_CELCE	5.15e-23	118	446	104	416	Glucan endo-1,3-beta-glucosidase OS=Cellulosimicrobium cellulans OX=1710 PE=1 SV=1
sp|Q59146|E13B_ARTSW	2.15e-22	118	406	104	377	Glucan endo-1,3-beta-glucosidase OS=Arthrobacter sp. (strain YCWD3) OX=79671 GN=glcI PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000010	0.000036

TMHMM  Annotations     

There is no transmembrane helices in EPE06073.1.