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CAZyme Information: MGYG000003252_00247

You are here: Home > Sequence: MGYG000003252_00247

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 Bacteroides sp900761785
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900761785
CAZyme ID MGYG000003252_00247
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1339 MGYG000003252_12|CGC3 151644.51 6.8931
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003252 8296673 MAG United States North America
Gene Location Start: 46607;  End: 50626  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.111 3.2.1.51

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 160 500 1.1e-120 0.973293768545994
GH29 788 1110 3.7e-82 0.869942196531792
CBM32 1235 1337 1.1e-16 0.75

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06563 GH20_chitobiase-like 0.0 165 513 1 357
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
pfam00728 Glyco_hydro_20 2.42e-163 165 500 1 345
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525 Chb 3.14e-125 102 605 203 716
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06570 GH20_chitobiase-like_1 8.92e-101 165 513 1 311
A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This subgroup lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
cd06568 GH20_SpHex_like 1.01e-92 165 513 1 329
A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRP58722.1 8.37e-318 761 1339 24 602
QQT79395.1 8.37e-318 761 1339 24 602
ASM67352.1 8.37e-318 761 1339 24 602
QUU10050.1 6.69e-317 761 1339 24 602
QUT75447.1 1.69e-315 761 1338 16 593

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 2.50e-310 760 1338 4 582
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
6Q63_A 4.47e-149 16 616 24 627
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
3UES_A 9.94e-129 771 1213 4 475
Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UES_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3MO4_A 2.92e-127 771 1213 6 477
Thecrystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3MO4_B The crystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3UET_A 1.03e-126 771 1213 4 475
Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UET_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P49008 1.14e-229 18 756 32 770
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
B2UQG6 2.59e-110 89 530 81 532
Beta-hexosaminidase Amuc_0868 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_0868 PE=1 SV=1
Q7XUR3 3.39e-107 787 1203 39 465
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
Q8GW72 1.65e-105 787 1214 37 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
P96155 1.29e-78 21 494 139 601
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.586696 0.412695 0.000155 0.000178 0.000139 0.000145

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003252_00247.