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CAZyme Information: MGYG000002403_04338

You are here: Home > Sequence: MGYG000002403_04338

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 Robinsoniella peoriensis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella peoriensis
CAZyme ID MGYG000002403_04338
CAZy Family GH136
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2676 MGYG000002403_116|CGC4 292691.6 4.8332
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002403 7202103 Isolate not provided not provided
Gene Location Start: 121667;  End: 129697  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002403_04338.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH136 274 809 3.6e-101 0.9918533604887984
GH20 1379 1717 2.2e-58 0.9703264094955489

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06564 GH20_DspB_LnbB-like 1.13e-86 1385 1716 1 324
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.
pfam00728 Glyco_hydro_20 5.29e-40 1384 1717 1 344
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742 GH20_hexosaminidase 1.95e-35 1387 1717 2 303
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.
cd06563 GH20_chitobiase-like 4.35e-34 1384 1732 1 355
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.
COG3525 Chb 3.10e-29 1235 1727 136 624
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AYE35145.1 5.20e-151 272 962 34 749
AZS13470.1 1.10e-149 924 1951 17 931
SYX85460.1 7.06e-148 1000 1951 123 982
SQI04664.1 4.37e-146 965 1945 183 1093
ASY51670.1 5.88e-146 969 1945 187 1093

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JQF_A 4.13e-73 1141 1748 6 576
Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
7V6M_A 8.66e-37 272 815 8 581
ChainA, Fibronectin type III domain-containing protein [Tyzzerella nexilis]
7V6I_A 2.79e-28 274 807 14 605
ChainA, Lacto-N-biosidase [Bifidobacterium saguini DSM 23967]
5GQC_A 1.84e-27 267 807 12 593
Crystalstructure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_C Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_D Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_E Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_F Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_G Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQC_H Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, ligand-free form [Bifidobacterium longum subsp. longum],5GQF_A Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, lacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQF_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, lacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQG_A Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, galacto-N-biose complex [Bifidobacterium longum subsp. longum],5GQG_B Crystal structure of lacto-N-biosidase LnbX from Bifidobacterium longum subsp. longum, galacto-N-biose complex [Bifidobacterium longum subsp. longum]
3GH4_A 3.81e-26 1220 1731 22 502
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B2UPR7 4.08e-77 1141 1748 28 598
Beta-hexosaminidase Amuc_2136 OS=Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc) OX=349741 GN=Amuc_2136 PE=1 SV=1
P96155 1.14e-22 1340 1632 215 528
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
B2UP57 3.38e-18 1290 1617 33 355
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
P49008 2.97e-16 1288 1717 72 504
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q0TR53 1.41e-15 983 1136 631 776
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

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
0.258350 0.631672 0.104680 0.004430 0.000555 0.000313

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002403_04338.