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CAZyme Information: MGYG000000720_02012

You are here: Home > Sequence: MGYG000000720_02012

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis;
CAZyme ID MGYG000000720_02012
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
997 110680.37 6.6895
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000720 3759035 MAG Kazakhstan Asia
Gene Location Start: 11555;  End: 14548  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000720_02012.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 353 639 2.4e-24 0.728538283062645

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09621 CBM9_like_5 4.89e-77 809 997 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.
cd09619 CBM9_like_4 8.28e-14 834 982 30 175
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.
cd00241 DOMON_like 1.01e-09 832 978 10 157
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 4.84e-06 833 996 20 180
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.
pfam01229 Glyco_hydro_39 4.97e-05 333 639 55 385
Glycosyl hydrolases family 39.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHF94342.1 6.20e-263 14 997 36 1032
AHF90198.1 6.62e-237 42 997 41 1005
AVM47149.1 4.03e-178 200 997 498 1306
AVM46276.1 3.08e-176 202 997 336 1136
AVM44759.1 4.27e-161 293 997 254 964

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5JVK_A 3.27e-22 266 718 66 524
Structuralinsights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_B Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus],5JVK_C Structural insights into a family 39 glycoside hydrolase from the gut symbiont Bacteroides cellulosilyticus WH2. [Bacteroides cellulosilyticus]
4ZN2_A 6.43e-07 317 596 32 324
Glycosylhydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_B Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_C Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],4ZN2_D Glycosyl hydrolase from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1]
5BX9_A 6.43e-07 317 596 32 324
Structureof PslG from Pseudomonas aeruginosa [Pseudomonas aeruginosa PAO1],5BXA_A Structure of PslG from Pseudomonas aeruginosa in complex with mannose [Pseudomonas aeruginosa PAO1]

Swiss-Prot Hits      help

has no Swissprot hit.

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
0.000514 0.998732 0.000250 0.000165 0.000162 0.000158

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000720_02012.