CAZyme Information: MGYG000001787_02101

Basic Information

• Species: Phocaeicola sp900551645
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900551645
• CAZyme ID: MGYG000001787_02101
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
351	MGYG000001787_75|CGC1	40715.94	4.6503

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001787	3320861	MAG	Denmark	Europe

• Gene Location: Start: 13028; End: 14083 Strand: -

Full Sequence      

MKKLIYTCLLAMTALPALSQSLFEKYERFLTAPRTYTCFRTTGELNIDGKLDESSWLKAA
STEPFVDISGEGFPTPKYQTTAKMLWDDDYLYVGAILEEENIKAKLTQRDTIIYYDNDFE
VFIDPDNNGQGYFEFETNARGVLFDLILDKPYRTGGSFLIPWDCKDIKLAIHCEGTLNNP
TDKDKYWSVEMAIPHQAITWNFENPLKAGNIWRINFSRVQWLKEKGPEENWVWTPTGKVD
MHMPDRWGYLYLADSPVGSRIRVDWSPACPASIYKLMWAMFYAQQDAYGQNHSYLQSIDQ
FQITDKEREGLPTGTQIDLEASSNLYRITVTDPNTQTRYLLNNEGRFWSEK

Enzyme Prediction     

No EC number prediction in MGYG000001787_02101.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	47	252	2.5e-42	0.9945054945054945

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09620	CBM9_like_3	6.96e-75	47	249	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	3.95e-31	35	219	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.
pfam06452	CBM9_1	6.92e-11	47	145	1	94	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.
cd09619	CBM9_like_4	2.50e-07	46	143	3	99	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.
cd00005	CBM9_like_1	4.17e-06	47	134	11	89	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
AND21566.1	1.11e-186	1	351	1	350
QUT85170.1	1.11e-186	1	351	1	350
ALK86129.1	1.57e-186	1	351	1	350
QEW35857.1	1.57e-186	1	351	1	350
QJR73538.1	2.23e-186	1	351	1	350

PDB Hits     

has no PDB hit.

Swiss-Prot Hits     

has no Swissprot hit.

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
0.000469	0.998774	0.000212	0.000178	0.000171	0.000165

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001787_02101.