logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000588_00107

You are here: Home > Sequence: MGYG000000588_00107

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; Firmicutes; Bacilli; ML615J-28; CAG-313; UMGS75;
CAZyme ID MGYG000000588_00107
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
604 MGYG000000588_5|CGC1 70405.96 6.6109
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000588 1739916 MAG Madagascar Africa
Gene Location Start: 17686;  End: 19500  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000588_00107.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 118 426 1.4e-39 0.9554896142433235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 6.68e-73 119 425 1 301
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. 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.
cd06564 GH20_DspB_LnbB-like 9.27e-15 118 331 1 217
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. 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.
cd02742 GH20_hexosaminidase 1.92e-14 119 402 1 278
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) 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. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
pfam02838 Glyco_hydro_20b 1.10e-11 3 113 4 123
Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
cd06570 GH20_chitobiase-like_1 9.98e-10 120 270 4 158
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QVK17427.1 4.21e-168 2 597 3 610
QNK59368.1 2.31e-109 4 593 9 619
AYQ72904.1 1.42e-108 1 602 7 633
ACJ75922.1 2.84e-108 1 594 1 599
QJD87484.1 1.28e-107 1 594 6 620

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4H04_A 7.07e-16 63 425 102 475
Lacto-N-biosidasefrom Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4H04_B Lacto-N-biosidase from Bifidobacterium bifidum [Bifidobacterium bifidum JCM 1254],4JAW_A Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],4JAW_B Crystal Structure of Lacto-N-Biosidase from Bifidobacterium bifidum complexed with LNB-thiazoline [Bifidobacterium bifidum JCM 1254],5BXP_A LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXP_B LNBase in complex with LNB-LOGNAc [Bifidobacterium bifidum JCM 1254],5BXR_A LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXR_B LNBase in complex with LNB-NHAcDNJ [Bifidobacterium bifidum JCM 1254],5BXS_A LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXS_B LNBase in complex with LNB-NHAcCAS [Bifidobacterium bifidum JCM 1254],5BXT_A LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254],5BXT_B LNBase in complex with LNB-NHAcAUS [Bifidobacterium bifidum JCM 1254]
6YHH_A 5.20e-15 69 335 92 383
X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
7DUP_A 1.45e-12 3 335 6 389
ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_A Chain A, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVA_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
7DVB_A 5.86e-12 3 335 6 389
ChainA, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_B Chain B, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_C Chain C, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron],7DVB_D Chain D, Beta-N-acetylhexosaminidase [Bacteroides thetaiotaomicron]
6Q63_A 7.08e-11 69 269 106 333
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
E9DFH0 4.69e-15 69 336 122 415
Beta-hexosaminidase 1 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) OX=443226 GN=HEX1 PE=1 SV=1
Q0TR53 4.62e-08 5 121 48 183
O-GlcNAcase NagJ OS=Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A) OX=195103 GN=nagJ PE=1 SV=1
Q8XL08 4.62e-08 5 121 48 183
O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q9HGI3 4.07e-06 80 339 142 426
Beta-hexosaminidase OS=Emericella nidulans OX=162425 GN=nagA 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
1.000040 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000588_00107.