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CAZyme Information: MGYG000001400_03540

You are here: Home > Sequence: MGYG000001400_03540

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 Erysipelatoclostridium ramosum
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Erysipelatoclostridium; Erysipelatoclostridium ramosum
CAZyme ID MGYG000001400_03540
CAZy Family CBM32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1527 170051.84 4.3388
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001400 3785853 Isolate not provided not provided
Gene Location Start: 65730;  End: 70313  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001400_03540.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 562 901 1.5e-57 0.9673590504451038
CBM32 199 330 1.4e-24 0.9516129032258065
CBM32 51 184 1.3e-19 0.9354838709677419
CBM32 1133 1263 1.3e-17 0.9435483870967742

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06564 GH20_DspB_LnbB-like 1.83e-135 568 903 1 326
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 6.09e-32 570 902 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.
COG3525 Chb 1.72e-27 398 904 81 621
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
pfam00728 Glyco_hydro_20 3.45e-27 567 901 1 343
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
pfam02838 Glyco_hydro_20b 4.54e-26 437 563 1 123
Glycosyl hydrolase family 20, domain 2. This domain has a zincin-like fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQV05894.1 0.0 1 1527 1 1527
QPS14026.1 0.0 1 1527 1 1527
QMW75640.1 0.0 1 1527 1 1527
QQY27155.1 0.0 1 1527 1 1527
QMI86523.1 0.0 39 1333 30 1308

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JQF_A 1.33e-121 349 1103 3 724
Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4H04_A 2.18e-29 437 908 33 487
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]
4A41_A 5.09e-26 1129 1265 29 159
CpGH89CBM32-5,from Clostridium perfringens, in complex with galactose [Clostridium perfringens],4A44_A CpGH89CBM32-5, from Clostridium perfringens, in complex with the Tn Antigen [Clostridium perfringens],4A45_A CpGH89CBM32-5, from Clostridium perfringens, in complex with GalNAc- beta-1,3-galactose [Clostridium perfringens],4AAX_A CpGH89CBM32-5, from Clostridium perfringens, in complex with N- acetylgalactosamine [Clostridium perfringens]
3GH4_A 1.06e-24 436 846 37 447
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]
6Z14_JJJ 4.24e-21 193 684 20 442
ChainJJJ, Beta-N-acetylhexosaminidase [Bifidobacterium bifidum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B2UPR7 3.20e-126 349 1110 25 753
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
P49008 1.42e-18 440 692 37 283
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
P13670 1.30e-14 470 724 230 495
N,N'-diacetylchitobiase OS=Vibrio harveyi OX=669 GN=chb PE=1 SV=1
P96155 1.58e-14 371 690 88 380
Beta-hexosaminidase OS=Vibrio furnissii OX=29494 GN=exoI PE=1 SV=1
P0CS93 2.79e-13 1125 1270 50 191
Galactose oxidase OS=Gibberella zeae OX=5518 GN=GAOA 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
0.000292 0.998939 0.000183 0.000211 0.000190 0.000168

TMHMM  Annotations      download full data without filtering help

start end
9 31
1501 1520