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CAZyme Information: MGYG000000839_01614

You are here: Home > Sequence: MGYG000000839_01614

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 Clostridium sp900540255
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium sp900540255
CAZyme ID MGYG000000839_01614
CAZy Family GH20
CAZyme Description Beta-N-acetylhexosaminidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
535 MGYG000000839_18|CGC2 61141.67 5.247
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000839 2735655 MAG China Asia
Gene Location Start: 13757;  End: 15364  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000839_01614.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 190 504 3.1e-102 0.9762611275964391

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06568 GH20_SpHex_like 0.0 196 517 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.
cd06563 GH20_chitobiase-like 1.30e-133 196 517 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 3.98e-110 196 503 1 344
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742 GH20_hexosaminidase 8.87e-96 198 502 1 302
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.
COG3525 Chb 2.28e-78 130 532 200 643
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ACD51848.1 5.57e-267 13 535 27 540
AJF29368.1 5.57e-267 13 535 27 540
AJF32429.1 5.57e-267 13 535 27 540
ACD23696.1 5.38e-266 11 535 12 529
CDH90358.1 5.38e-266 11 535 12 529

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3GH4_A 7.54e-189 43 532 26 520
Crystalstructure of beta-hexosaminidase from Paenibacillus sp. TS12 [Paenibacillus sp.],3GH5_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GlcNAc [Paenibacillus sp.],3GH7_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with GalNAc [Paenibacillus sp.],3SUR_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NAG-thiazoline. [Paenibacillus sp. TS12],3SUS_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-NAG-thiazoline [Paenibacillus sp. TS12],3SUT_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc [Paenibacillus sp. TS12],3SUU_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with Gal-PUGNAc [Paenibacillus sp. TS12],3SUV_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-DNJ [Paenibacillus sp. TS12],3SUW_A Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with NHAc-CAS [Paenibacillus sp. TS12]
1HP4_A 2.48e-139 55 533 27 505
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 1.40e-138 55 533 27 505
ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
1M03_A 3.97e-138 55 533 27 505
ChainA, Beta-N-acetylhexosaminidase [Streptomyces plicatus]
4C7D_A 3.24e-135 55 533 9 487
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q7WUL4 3.15e-99 53 517 4 463
Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 PE=1 SV=1
P49008 3.39e-84 53 532 35 533
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P96155 3.26e-62 53 505 139 608
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UQG6 9.67e-62 134 531 95 529
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
B2UP57 8.78e-50 131 517 53 462
Beta-hexosaminidase Amuc_2018 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2018 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
0.666511 0.317485 0.004628 0.001091 0.000606 0.009688

TMHMM  Annotations      download full data without filtering help

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