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CAZyme Information: MGYG000001735_01188

You are here: Home > Sequence: MGYG000001735_01188

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; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae; Parabacteroides;
CAZyme ID MGYG000001735_01188
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
683 MGYG000001735_10|CGC1 78616.24 5.9931
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001735 5309957 MAG Sweden Europe
Gene Location Start: 47629;  End: 49680  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001735_01188.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 141 466 4.5e-40 0.9703264094955489

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 7.66e-78 147 465 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.
COG3525 Chb 3.36e-23 20 328 129 488
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam02838 Glyco_hydro_20b 1.92e-17 26 141 3 123
Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.
cd06568 GH20_SpHex_like 6.57e-15 146 475 2 326
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.
pfam00728 Glyco_hydro_20 1.08e-14 146 329 2 222
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUT49641.1 0.0 5 682 6 683
ADV43364.1 0.0 11 683 12 684
QQY39583.1 0.0 2 683 3 684
ABR38110.1 0.0 2 683 3 684
QQY42843.1 0.0 2 683 3 684

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1HP4_A 1.07e-23 68 471 76 503
ChainA, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1HP5_A Chain A, Beta-n-acetylhexosaminidase [Streptomyces plicatus],1JAK_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],1M01_A Chain A, Beta-N-acetylhexosaminidase [Streptomyces plicatus],5FCZ_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus],5FD0_A Chain A, B-N-acetylhexosaminidase [Streptomyces plicatus]
1M04_A 4.52e-23 68 471 76 503
ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
6Q63_A 8.15e-23 89 329 103 391
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]
4C7D_A 9.46e-23 68 380 58 390
Structureand activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7D_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_A Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor],4C7F_B Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2) [Streptomyces coelicolor]
1M03_A 1.07e-22 68 471 76 503
ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P49008 1.10e-18 85 329 104 387
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q7WUL4 8.60e-17 28 327 7 346
Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
Q04786 2.89e-10 27 235 200 438
Beta-hexosaminidase OS=Vibrio vulnificus OX=672 GN=hex PE=3 SV=1
A6QNR0 1.37e-09 148 486 2 345
Hexosaminidase D OS=Bos taurus OX=9913 GN=HEXD PE=2 SV=2
Q3U4H6 4.09e-09 148 442 10 298
Hexosaminidase D OS=Mus musculus OX=10090 GN=Hexd 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
0.000379 0.998942 0.000190 0.000157 0.000158 0.000152

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001735_01188.