CAZyme Information: MGYG000000312_01850

Basic Information

• Species: Eisenbergiella sp900539715
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eisenbergiella; Eisenbergiella sp900539715
• CAZyme ID: MGYG000000312_01850
• CAZy Family: CBM9
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
352	MGYG000000312_19|CGC1	40391.14	4.393

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000312	2782709	MAG	Sweden	Europe

• Gene Location: Start: 21271; End: 22329 Strand: +

Full Sequence      

MSKINIPIPAVDFQPPVYVCRRAAGEFTLDGRLDKPFWENAPWTDAFLDIEGSHMPLPRF
LTRAKMLWDDENIYFGAQLDGDEIWGHITQRDAVIFHDNDFEIFIDPDSDTQQYYEFEMN
VLNTVWDLFLPIAYRDGGDALNGFDYHGLRTAVHVDGDINDPSAKNNFWSVEVVIPFASL
NECIPNQPVPKSGDFYRLNFSRVQWKVDVEESAFHKRTGENGRPLPEDNWVWAPTGVINI
HYPELWGFLFFADADADDAAFAIPEDEKRKWELRKLYYAEKIHFDLHGSYTADLGVLKGI
LKEYAPNEKNVSVRDDLTYTVETTSHGFELSCPAEEDGHNIVLFGNGKVKKI

Enzyme Prediction     

No EC number prediction in MGYG000000312_01850.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	30	206	5.8e-34	0.8241758241758241

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09620	CBM9_like_3	7.20e-65	29	248	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	2.06e-21	17	203	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	2.54e-08	51	180	9	127	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	3.43e-07	29	180	1	132	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCJ97215.1	3.90e-187	1	350	1	350
QLG42346.1	1.55e-131	1	351	1	339
QOS77319.1	4.42e-131	1	351	1	339
QOT09656.1	4.58e-131	1	349	1	338
QZN78207.1	2.93e-129	1	351	1	339

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
1.000029	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000312_01850.