CAZyme Information: MGYG000001526_02379

Basic Information

• Species: Paenibacillus_A senegalimassiliensis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A senegalimassiliensis
• CAZyme ID: MGYG000001526_02379
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
360	MGYG000001526_14|CGC3	42003.04	4.6366

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001526	5059338	Isolate	not provided	not provided

• Gene Location: Start: 396924; End: 398006 Strand: +

Full Sequence      

MANESLSSTSQGGDKLRYSEVPEPQLPFAPKSYICRRAAGELELDGRIEKPFWATAAWTE
DFVDIEGHLRPHPAKRTRVKMLWDDDYFYIAAEMEEDEIWATLQERDTVIFHDNDFEIFI
DPDGDTHLYYELEVNALNTVWDLLLPKPYRDGGPPVNGWDIQGLRSAVFIDGELNHPQAD
NRRWSVEVALPWKALKECAPEGRMPKVGEYWRVNFSRVEWQVEVKDGQYVKLINPDTGNP
YPEANWVWSPQGVINMHYPEMWGFIVFTEADASESINFTLPRDEIIKWELRRLYYRQRHH
YASHGHFADDLTRLKVEPSGEEFYPALEAAGRIFLISSPSADGRHKWYIREDGQLWKEPI

Enzyme Prediction     

No EC number prediction in MGYG000001526_02379.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	45	226	2.4e-40	0.8516483516483516

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09620	CBM9_like_3	1.57e-71	44	264	1	200	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.
cd09618	CBM9_like_2	2.74e-25	32	218	1	170	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized subfamily are typically found at the N-terminus of longer proteins that lack additional annotation with domain footprints.
cd00241	DOMON_like	1.12e-10	61	215	4	142	Domon-like ligand-binding domains. DOMON-like domains can be found in all three kindgoms of life and are a diverse group of ligand binding domains that have been shown to interact with sugars and hemes. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.
pfam06452	CBM9_1	4.75e-09	44	196	1	133	Carbohydrate family 9 binding domain-like. CBM9_1 is a C-terminal domain on bacterial xylanase proteins, and it is tandemly repeated in a number of family-members. The CBM9 module binds to amorphous and crystalline cellulose and a range of soluble di- and monosaccharides as well as to cello- and xylo- oligomers of different degrees of polymerization. Comparison of the glucose and cellobiose complexes during crystallisation reveals surprising differences in binding of these two substrates by CBM9-2. Cellobiose was found to bind in a distinct orientation from glucose, while still maintaining optimal stacking and electrostatic interactions with the reducing end sugar.
cd00005	CBM9_like_1	2.05e-04	43	140	10	103	DOMON-like type 9 carbohydrate binding module of xylanases. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. The CBM9 domain frequently occurs in tandem repeats; members found in this subfamily typically co-occur with glycosyl hydrolase family 10 domains and are annotated as endo-1,4-beta-xylanases. CBM9 from Thermotoga maritima xylanase 10A is reported to have specificity for polysaccharide reducing ends.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QYR24058.1	6.82e-186	16	358	1	342
QOT09656.1	2.40e-185	19	358	4	341
QLG42346.1	1.21e-180	16	358	1	340
QOS77319.1	1.71e-180	16	358	1	340
QZN78207.1	4.01e-179	19	358	4	340

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000072	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001526_02379.