CAZyme Information: MGYG000001884_01297

Basic Information

• Species: UBA1829 sp900760615
• Lineage: Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900760615
• CAZyme ID: MGYG000001884_01297
• CAZy Family: GH0
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
619		69043.64	8.3518

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001884	3294047	MAG	Denmark	Europe

• Gene Location: Start: 3334; End: 5193 Strand: -

Full Sequence      

MWKPHVATGAALLLDFAGGMPPWTRPGPDTPRGTVLPLNCDPARFREHFEHLADFIASMP
SIRYFEWINEPNLSRIYRTGMYCEALRQLYPILKAKNPALKVGTGGLVVNHPSVTPGFAE
QVYGDMKDCYDIAFYHAHSGYRRYILDTRAASSLLPGRKPLANTEAGYRSYQGTPHLFYN
QARELVKKITVSKATGLEFYIWFMLQDYWDKYRNADDSFGLVTVDNQPKPSFAAYNELIR
QLSNTTPAGASKLHAELEGWQFLTGKEEVHVLWPKQDGTVHTLCLETDQDILLTDLFGNE
RRFHPADGIVALPTPELPFYLRAPEGAVKPAGALLTFAERPVRLPGPDTPLNAELHNPFR
ETVRCTLTDDTGKQHNATLAGKSSARITLPCALPAGTAPGPVIRQAKIVMARPDGKTVYS
GTFRFPVSAALPVRETAGPVIALNSEKQLMELAFDPTTPRWGGKTDLSARIRIRRDAKDL
IFNAEVSDNDHSVPHKNESIWKNDSLQIAIADEQGRMTEFTVSGQADAPAVAWRHIAPDE
NRTGRFHIPLTVNRGGGVTRYRFSVPFSELGISPVKGTRFRLAFLVNDNDSGKRLRIMEY
FKGIEGTKNPELFGWCILD

Enzyme Prediction     

No EC number prediction in MGYG000001884_01297.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09621	CBM9_like_5	7.21e-44	439	618	1	188	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 functional domains such as glycosyl hydrolases. The CBM9 module in these architectures may be involved in binding to carbohydrates.
cd00241	DOMON_like	3.76e-10	452	600	3	158	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.
cd09619	CBM9_like_4	3.90e-10	461	592	30	163	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	3.57e-06	456	618	16	181	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
AVM46501.1	1.65e-207	1	618	532	1153
AHF92778.1	1.41e-151	3	619	554	1178
AVM46714.1	3.03e-137	1	614	349	964
AVM46712.1	1.81e-130	1	614	398	1007
AVM46271.1	2.03e-95	3	618	356	965

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
0.760407	0.238775	0.000412	0.000138	0.000121	0.000145

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001884_01297.