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CAZyme Information: MGYG000003882_00460

You are here: Home > Sequence: MGYG000003882_00460

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; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Klebsiella;
CAZyme ID MGYG000003882_00460
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
797 MGYG000003882_28|CGC1 88911.44 5.6254
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003882 3911502 MAG United States North America
Gene Location Start: 8754;  End: 11147  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.52

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 157 587 6.6e-122 0.973293768545994

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06570 GH20_chitobiase-like_1 1.80e-173 162 600 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.
cd06563 GH20_chitobiase-like 4.29e-134 162 600 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 7.42e-118 162 587 1 345
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd06562 GH20_HexA_HexB-like 6.31e-107 162 603 1 340
Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. 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.
COG3525 Chb 8.46e-84 15 412 117 539
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QVJ10661.1 0.0 1 797 1 797
ATX86026.1 0.0 1 797 1 797
QHJ54117.1 0.0 1 797 1 797
QII33357.1 0.0 1 797 1 797
QEU20249.1 0.0 1 797 1 797

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6YHH_A 1.32e-112 27 791 6 672
X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
7CBN_A 1.65e-72 110 600 78 496
Crystalstructure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835],7CBO_A Crystal structure of beta-N-acetylhexosaminidase Am0868 from Akkermansia muciniphila in complex with GlcNAc [Akkermansia muciniphila ATCC BAA-835]
6Q63_A 1.80e-65 107 429 103 448
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
1NOU_A 6.72e-65 30 600 7 480
Nativehuman lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOU_B Native human lysosomal beta-hexosaminidase isoform B [Homo sapiens],1NOW_A Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],1NOW_B Human lysosomal beta-hexosaminidase isoform B in complex with (2R,3R,4S,5R)-2-Acetamido-3,4-Dihydroxy-5-Hydroxymethyl-Piperidinium Chloride (GalNAc-isofagomine) [Homo sapiens],2GJX_B Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_C Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_F Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens],2GJX_G Crystallographic structure of human beta-Hexosaminidase A [Homo sapiens]
3LMY_A 7.71e-65 8 600 28 529
TheCrystal Structure of beta-hexosaminidase B in complex with Pyrimethamine [Homo sapiens],3LMY_B The Crystal Structure of beta-hexosaminidase B in complex with Pyrimethamine [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B2UQG6 1.17e-71 110 600 97 515
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
P49008 8.05e-70 34 412 39 432
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155 2.21e-67 14 412 114 532
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P20060 4.12e-67 9 600 13 508
Beta-hexosaminidase subunit beta OS=Mus musculus OX=10090 GN=Hexb PE=1 SV=2
P49614 9.46e-66 92 600 103 503
Beta-hexosaminidase subunit beta OS=Felis catus OX=9685 GN=HEXB PE=2 SV=2

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
0.000328 0.998896 0.000184 0.000216 0.000183 0.000157

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003882_00460.