dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Victivallis sp900761715

Lineage

Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp900761715

CAZyme ID

MGYG000003249_00965

CAZy Family

GH50

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1095	MGYG000003249_173\|CGC1	121897.65	5.8609

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003249	2933905	MAG	United States	North America

Gene Location

Start: 1454; End: 4741 Strand: -

Enzyme Prediction help

No EC number prediction in MGYG000003249_00965.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH50	392	872	4.1e-87	0.781010719754977
CBM9	926	1093	4.4e-24	0.9010989010989011

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd09619	CBM9_like_4	3.09e-23	908	1095	4	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	2.29e-16	907	1094	4	182	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.
cd00005	CBM9_like_1	4.06e-15	932	1094	32	185	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.
cd00241	DOMON_like	1.48e-13	935	1075	16	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.
cd09621	CBM9_like_5	7.74e-13	936	1093	27	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AVM47142.1	6.33e-286	212	1095	23	906
SDU06021.1	3.16e-177	215	1093	45	937
AHF90550.1	1.09e-176	398	1094	1	717
SDU02961.1	7.16e-176	206	1095	22	940
SDT95096.1	1.81e-164	398	1094	38	756

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6XJ9_A	1.32e-45	398	873	223	760	Structureof PfGH50B [Pseudoalteromonas fuliginea],6XJ9_B Structure of PfGH50B [Pseudoalteromonas fuliginea]
5Z6P_A	3.14e-45	338	872	151	759	Thecrystal structure of an agarase, AgWH50C [Agarivorans gilvus],5Z6P_B The crystal structure of an agarase, AgWH50C [Agarivorans gilvus]
4BQ2_A	1.16e-44	231	879	29	750	Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ2_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_C Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ3_D Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40]
4BQ4_A	2.76e-44	231	879	29	750	Structuralanalysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ4_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_A Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40],4BQ5_B Structural analysis of an exo-beta-agarase [Saccharophagus degradans 2-40]
5T3B_A	6.69e-11	451	875	92	476	ChainA, Glycoside Hydrolase [Phocaeicola plebeius],5T3B_B Chain B, Glycoside Hydrolase [Phocaeicola plebeius]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48840	4.03e-44	398	872	432	949	Beta-agarase B OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaB PE=3 SV=1
P48839	5.88e-28	399	872	400	913	Beta-agarase A OS=Vibrio sp. (strain JT0107) OX=47913 GN=agaA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000686	0.937501	0.061051	0.000278	0.000258	0.000202

TMHMM Annotations help

There is no transmembrane helices in MGYG000003249_00965.

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