CAZyme Information: MGYG000003367_00416

Basic Information

• Species: Bacteroides sp007896885
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp007896885
• CAZyme ID: MGYG000003367_00416
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
369	MGYG000003367_13|CGC2	42908.58	6.1787

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003367	3747359	MAG	United States	North America

• Gene Location: Start: 121397; End: 122506 Strand: +

Full Sequence      

MKKKFLSLFVFITALYGEVNAQALSDKYAPMLTIPKGYVCYRTADAIHVDGLANEASWKN
AQPTEAFVDISGYHFPTPRYQTTAKMLWDDKYLYIFAELEEPHIWANLQKRDTIVFYDND
FEVFIDPIGEGHNYFEIETNAIGTVFDLSLEKPYRAPRRTFVQFQWNCPGLKLATHCVGK
INNSKGTDKGWTVEMAIPREAIASEFDNYLKAGQWLRINFSRVEWQYDIDANGRYDRKKG
KDGKYLPEDNWVWSPTGQIAMHMPERWGYMYFSDKTVGQGTDTFRYPTDEPVRRFLNMLF
YAQEEQYAKTKSYYKELKDFGLQPKDMQMLPAGYQVNVETTSHTYEITALSPEGKAYVMN
ESGSCFIRK

Enzyme Prediction     

No EC number prediction in MGYG000003367_00416.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	49	230	7.6e-40	0.8516483516483516

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09620	CBM9_like_3	1.37e-70	49	269	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	9.00e-21	38	223	2	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.
cd09619	CBM9_like_4	7.26e-12	46	268	1	187	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 are often located at the C-terminus of longer proteins and may co-occur with various other domains.
pfam06452	CBM9_1	1.57e-10	49	268	1	177	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.
cd00241	DOMON_like	1.14e-06	74	201	12	126	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAH07622.1	1.46e-123	1	369	11	358
QCT78438.1	1.46e-123	1	369	11	358
CBW22417.1	4.10e-123	1	369	11	358
QRP90424.1	8.17e-123	1	369	11	358
AKA51642.1	8.17e-123	1	369	11	358

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P36917	2.05e-06	12	202	831	994	Endo-1,4-beta-xylanase A OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=xynA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000273	0.999044	0.000184	0.000172	0.000168	0.000147

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003367_00416.