CAZyme Information: KAF6519152.1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: KAF6519152.1
• CAZy Family: GH134
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578	CM024368|CGC9	63474.24	5.6000

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo5176	17912	660025	0	17912

• Gene Location: location=CM024368:1916907-1919589(-)

Full Sequence      

MIFSLTHLLVTARLVSGACECGYSIKNPQGDSPIVFTDRLETKFSQLHKISEGHDWVAQN
FTVSAADGRGNFSKAFLPTNVNTRGTKSGDDSGLELRYFNDTQEIDIEFLSQEFDHDNGI
YPINLVVQSKKSLEAGYDASKTGSFKRVRLDFDPTDAFHEYRFDYLPGQVLFYADGKLLA
RMKGGDMPSSGGHLILQHWKPFLDIILTNHTDSKSLFAHVTGRDEQGVLILLADGETVHR
PKSPSEILQPVGADIAIPVGGPGAQKKVRIPHIFGGRIWFCKDKPLTFLINPGPAVVEPS
VTNPTDPNFDADWGFCEFTYNNDQLYVNVSYVDFVSIPIGLELENEAGQVMRVPGMPKDG
LDQVCEGLKRQGEKDGAGWEKLVVKSKSGSNLRALSPNAGAELHPGLLENYFAPEVDAAW
KRYEKEDIEINTQAEWGDVKGRVHDAKLVFKDVGRDKLSFHFEKPSTRDIVSCSTGPFAG
GPDVTPAQLNVGARIAAALNRTTLSGNSRQPEGEKVEEYYCKGEGKTNHYSRVCHEVTLE
GKGYAFPYDDVGASGGVDQSGFLNDGRPKVLTVHVGGQ

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH64	204	576	2.2e-105	0.9863760217983651
GH16	98	199	6.2e-46	0.5260416666666666

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
185759	GH64-GluB-like	0.0	203	576	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	8.79e-179	201	575	1	370	Beta-1,3-glucanase. Family 64 glycoside hydrolases have beta-1,3-glucanase activity.
185755	GH64-LPHase-like	8.08e-79	203	573	1	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	9.13e-39	203	576	3	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.
185683	Glyco_hydrolase_16	8.99e-19	101	199	97	184	glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD58554.1|GH64	3.84e-281	200	578	4	382
QGI98025.1|GH64	1.70e-276	188	578	34	424
QGI67139.1|GH64	1.70e-276	188	578	34	424
CCT71403.1|GH64	4.05e-276	200	578	4	382
QGI84374.1|GH64	2.52e-266	212	578	10	376

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3GD0_A	5.33e-37	254	569	59	357	Chain A, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis],3GD9_A Chain A, Laminaripentaose-producing beta-1,3-guluase (LPHase) [Streptomyces matensis]
5H9X_A	4.57e-12	268	576	211	443	Crystal structure of GH family 64 laminaripentaose-producing beta-1,3-glucanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii]
1CPN_A	3.13e-06	104	218	47	146	NATIVE-LIKE IN VIVO FOLDING OF A CIRCULARLY PERMUTED JELLYROLL PROTEIN SHOWN BY CRYSTAL STRUCTURE ANALYSIS [Paenibacillus macerans]
1MAC_A	3.29e-06	104	218	103	202	Crystal Structure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans],1MAC_B Crystal Structure And Site-Directed Mutagenesis Of Bacillus Macerans Endo-1,3-1,4-Beta-Glucanase [Paenibacillus macerans]
1AJK_A	3.36e-06	104	218	22	121	Circularly Permuted (1-3,1-4)-Beta-D-Glucan 4- Glucanohydrolase Cpa16m-84 [Paenibacillus macerans],1AJK_B Circularly Permuted (1-3,1-4)-Beta-D-Glucan 4- Glucanohydrolase Cpa16m-84 [Paenibacillus macerans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P22222|E13B_CELCE	9.48e-28	268	573	105	392	Glucan endo-1,3-beta-glucosidase OS=Cellulosimicrobium cellulans OX=1710 PE=1 SV=1
sp|Q59146|E13B_ARTSW	7.45e-27	268	573	105	392	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
0.764323	0.235685

TMHMM  Annotations     

There is no transmembrane helices in KAF6519152.1.