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CAZyme Information: MGYG000004510_00284

You are here: Home > Sequence: MGYG000004510_00284

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 Prevotella sp002481295
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp002481295
CAZyme ID MGYG000004510_00284
CAZy Family GH16
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
369 MGYG000004510_3|CGC2 40001.68 4.8109
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004510 3097673 MAG Israel Asia
Gene Location Start: 96273;  End: 97382  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004510_00284.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH16 137 364 1.6e-73 0.9956521739130435

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd08023 GH16_laminarinase_like 2.75e-88 137 364 1 235
Laminarinase, member of the glycosyl hydrolase family 16. Laminarinase, also known as glucan endo-1,3-beta-D-glucosidase, is a glycosyl hydrolase family 16 member that hydrolyzes 1,3-beta-D-glucosidic linkages in 1,3-beta-D-glucans such as laminarins, curdlans, paramylons, and pachymans, with very limited action on mixed-link (1,3-1,4-)-beta-D-glucans.
cd02182 GH16_Strep_laminarinase_like 1.54e-42 132 365 1 259
Streptomyces laminarinase-like, member of glycosyl hydrolase family 16. Proteins similar to Streptomyces sioyaensis beta-1,3-glucanase (laminarinase) present in Actinomycetales as well as Peziomycotina. Laminarinases belong to glycosyl hydrolase family 16 and hydrolyze the glycosidic bond of the 1,3-beta-linked glucan, a major component of fungal and plant cell walls and the structural and storage polysaccharides (laminarin) of marine macro-algae. Members of the GH16 family have a conserved jelly roll fold with an active site channel.
cd00413 Glyco_hydrolase_16 2.45e-34 139 364 1 210
glycosyl hydrolase family 16. The O-Glycosyl hydrolases are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A glycosyl hydrolase classification system based on sequence similarity has led to the definition of more than 95 different families inlcuding glycosyl hydrolase family 16. Family 16 includes lichenase, xyloglucan endotransglycosylase (XET), beta-agarase, kappa-carrageenase, endo-beta-1,3-glucanase, endo-beta-1,3-1,4-glucanase, and endo-beta-galactosidase, all of which have a conserved jelly roll fold with a deep active site channel harboring the catalytic residues.
cd08024 GH16_CCF 1.35e-26 135 365 1 330
Coelomic cytolytic factor, member of glycosyl hydrolase family 16. Subgroup of glucanases of unknown function that are related to beta-GRP (beta-1,3-glucan recognition protein), but contain active site residues. Beta-GRPs are one group of pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. Beta-GRPs are present in insects and lack all catalytic residues. This subgroup contains related proteins that still contain the active site and are widely distributed in eukaryotes. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic residues, like those of other glycosyl hydrolase family 16 members.
cd14948 BACON 8.64e-22 34 120 1 83
Bacteroidetes-Associated Carbohydrate-binding (putative) Often N-terminal (BACON) domain. The BACON domain is found in diverse domain architectures and accociated with a wide variety of domains, including carbohydrate-active enzymes and proteases. It was named for its suggested function of carbohydrate binding; the latter was inferred from domain architectures, sequence conservation, and phyletic distribution. However, recent experimental data suggest that its primary function in Bacteroides ovatus endo-xyloglucanase BoGH5A is to distance the catalytic module from the cell surface and confer additional mobility to the catalytic domain for attack of the polysaccharide. No evidence for a direct role in carbohydrate binding could be found in that case. The large majority of BACON domains are found in Bacteroidetes.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCS85683.1 1.18e-136 32 366 118 448
QUT92859.1 4.00e-123 35 366 122 452
SIP56442.1 2.20e-122 35 368 163 495
ALJ61571.1 3.01e-117 51 366 135 451
ADE81965.1 1.68e-115 10 366 5 360

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3ILN_A 5.19e-63 133 365 5 248
ChainA, Laminarinase [Rhodothermus marinus],3ILN_B Chain B, Laminarinase [Rhodothermus marinus]
5WUT_A 3.12e-60 132 365 4 235
Crystalstructure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.],5WUT_B Crystal structure of laminarinase from Flavobacterium sp. UMI-01 [Flavobacterium sp.]
6XOF_A 2.84e-54 130 366 21 268
ChainA, GH16 family protein [uncultured bacterium]
6XQF_A 1.57e-53 130 366 21 268
ChainA, GH16 family protein [uncultured bacterium],6XQG_A Chain A, GH16 family protein [uncultured bacterium],6XQH_A Chain A, GH16 family protein [uncultured bacterium],6XQL_A Chain A, GH16 family protein [uncultured bacterium],6XQM_A Chain A, GH16 family protein [uncultured bacterium]
4CRQ_A 7.99e-50 133 366 3 232
Crystalstructure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S [Zobellia galactanivorans],4CRQ_B Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S [Zobellia galactanivorans],4CTE_A Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S in complex with a thio-oligosaccharide [Zobellia galactanivorans],4CTE_B Crystal structure of the catalytic domain of the modular laminarinase ZgLamC mutant E142S in complex with a thio-oligosaccharide [Zobellia galactanivorans]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P45798 2.62e-63 128 365 35 283
Beta-glucanase OS=Rhodothermus marinus OX=29549 GN=bglA PE=1 SV=1
P23903 1.22e-40 129 366 419 681
Glucan endo-1,3-beta-glucosidase A1 OS=Niallia circulans OX=1397 GN=glcA PE=1 SV=1
Q27082 1.58e-37 133 368 25 256
Clotting factor G alpha subunit OS=Tachypleus tridentatus OX=6853 PE=1 SV=1
C1IE32 5.78e-34 135 362 22 265
Glucan endo-1,3-beta-glucosidase OS=Cryptopygus antarcticus OX=187623 PE=1 SV=1
Q9ZG90 5.08e-30 129 365 52 288
Keratan-sulfate endo-1,4-beta-galactosidase OS=Sphingobacterium multivorum OX=28454 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000049 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004510_00284.