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CAZyme Information: MGYG000000675_01047

You are here: Home > Sequence: MGYG000000675_01047

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 congonensis
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides congonensis
CAZyme ID MGYG000000675_01047
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1349 MGYG000000675_15|CGC1 153003.96 6.6357
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000675 5782172 MAG Kazakhstan Asia
Gene Location Start: 28165;  End: 32214  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 170 510 1.3e-119 0.973293768545994
GH29 798 1120 5.7e-82 0.869942196531792

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06563 GH20_chitobiase-like 0.0 175 523 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 2.04e-161 175 510 1 345
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
COG3525 Chb 9.95e-126 112 631 203 729
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd06570 GH20_chitobiase-like_1 2.37e-100 175 523 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 8.73e-92 175 523 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 1.92e-316 771 1349 24 602
QQT79395.1 1.92e-316 771 1349 24 602
ASM67352.1 1.92e-316 771 1349 24 602
QUU10050.1 1.10e-315 771 1349 24 602
QNL38600.1 4.39e-315 770 1348 23 601

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4ZRX_A 9.66e-310 770 1348 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 4.14e-147 26 626 24 627
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
3UES_A 1.12e-130 781 1223 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 3.29e-129 781 1223 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 1.16e-128 781 1223 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 1.43e-226 28 760 32 764
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q7XUR3 7.68e-109 797 1213 39 465
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
B2UQG6 1.45e-108 112 540 94 532
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
Q8GW72 6.98e-106 797 1224 37 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
P96155 1.18e-77 31 504 139 601
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000231 0.999100 0.000182 0.000163 0.000149 0.000144

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000675_01047.