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CAZyme Information: MGYG000000360_00996

You are here: Home > Sequence: MGYG000000360_00996

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 UBA1829 sp900548385
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA1829; UBA1829 sp900548385
CAZyme ID MGYG000000360_00996
CAZy Family GH39
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
986 111660.91 9.5247
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000360 4492877 MAG Sweden Europe
Gene Location Start: 283245;  End: 286205  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000360_00996.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH39 352 629 3.2e-19 0.7169373549883991

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd09621 CBM9_like_5 9.21e-55 797 983 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 1.06e-10 820 961 28 167
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 1.63e-08 822 963 12 156
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.
cd21510 agarase_cat 5.92e-06 395 469 81 163
alpha-beta barrel catalytic domain of agarase, such as GH86-like endo-acting agarases identified in non-marine organisms. Typically, agarases (E.C. 3.2.1.81) are found in ocean-dwelling bacteria since agarose is a principle component of red algae cell wall polysaccharides. Agarose is a linear polymer of alternating D-galactose and 3,6-anhydro-L-galactopyranose. Endo-acting agarases, such as glycoside hydrolase 16 (GH16) and GH86 hydrolyze internal beta-1,4 linkages. GH86-like endo-acting agarase of this protein family has been identified in the human intestinal bacterium Bacteroides uniformis. This acquired metabolic pathway, as demonstrated by the prevalence of agar-specific genetic cluster called polysaccharide utilization loci (PULs), varies considerably between human populations, being much more prevalent in a Japanese sample than in North America, European, or Chinese samples. Agarase activity was also identified in the non-marine bacterium Cellvibrio sp.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM46276.1 1.86e-183 163 984 306 1137
AVM47149.1 5.17e-174 36 984 200 1307
AHF94342.1 2.52e-161 50 985 83 1034
AVM44759.1 1.08e-152 189 984 160 965
AHF90198.1 4.80e-137 7 983 11 1005

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5JVK_A 8.74e-13 304 733 107 581
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]

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
0.000323 0.999039 0.000176 0.000150 0.000142 0.000139

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000360_00996.