CAZyme Information: MGYG000001512_01885

Basic Information

• Species: Coprobacter secundus
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter secundus
• CAZyme ID: MGYG000001512_01885
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
352	MGYG000001512_18|CGC16	39416.3	4.3846

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001512	4253015	Isolate	not provided	not provided

• Gene Location: Start: 1151075; End: 1152133 Strand: -

Full Sequence      

MKKFLCSLFSAVLLSSGISVWAQQDLTIKKVSAENAAISMDGSADEPIWSQIEAIPIDKP
FKQNETVTEEPSVTAYFKMFYQEDKTNSKYNYLYVYIDVTDDVLYPLWKNPDDVKNKHIY
DKVEVYLDVNDVLNDGKSPAYVNGHMDKGHFQMAPDMDDEYGYGYVTYPSGLLYGSLSEQ
VGVAYQLKSDGTGYGIEFEFPLNAFTNDKDEALSIEAFQNLPQGMGFDVVIVDNDNDGKG
RKRMAWKKNGPVEPYNNMDNCGVVRFGDEGGTVGIFETKKDISAVRVYPNPVVDLLTIEG
DFDNVSIFNSLGQKVKSDSNSIVNMEDVVSGIYIVKTYKDGKCNGYTKVMKK

Enzyme Prediction     

No EC number prediction in MGYG000001512_01885.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	41	262	2.6e-17	0.967032967032967

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam06452	CBM9_1	5.44e-13	41	246	2	162	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	1.13e-10	37	246	1	172	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.
pfam18962	Por_Secre_tail	6.45e-08	287	336	1	58	Secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.
TIGR04183	Por_Secre_tail	1.22e-07	287	352	1	72	Por secretion system C-terminal sorting domain. Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.
cd00241	DOMON_like	1.07e-06	91	241	29	154	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
BCI63366.1	8.76e-262	1	352	1	352

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
0.001578	0.996018	0.001727	0.000244	0.000208	0.000191

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001512_01885.