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CAZyme Information: MGYG000001328_02935

You are here: Home > Sequence: MGYG000001328_02935

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 tertium
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium tertium
CAZyme ID MGYG000001328_02935
CAZy Family CBM32
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1616 MGYG000001328_3|CGC44 179827.43 4.4209
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001328 3807822 Isolate not provided not provided
Gene Location Start: 2774624;  End: 2779474  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001328_02935.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 571 905 2.3e-57 0.9495548961424333
CBM32 213 340 3.1e-26 0.9435483870967742
CBM32 1134 1259 1.1e-23 0.9435483870967742
CBM32 47 168 1.4e-20 0.8870967741935484

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06564 GH20_DspB_LnbB-like 3.80e-132 572 906 2 325
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 1.44e-31 573 905 4 343
Glycosyl hydrolase family 20, catalytic domain. This domain has a TIM barrel fold.
cd02742 GH20_hexosaminidase 3.10e-29 573 906 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 4.64e-27 573 916 4 353
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.
pfam00754 F5_F8_type_C 1.04e-21 214 340 1 127
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AYE33718.1 0.0 10 1551 11 1675
QAS61873.1 0.0 10 1551 11 1675
ATD55826.1 0.0 10 1551 11 1674
SLK21750.1 0.0 10 1551 11 1674
QBJ76126.1 0.0 10 1551 11 1674

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JQF_A 3.19e-134 353 1112 2 734
Crystallizationanalysis of a beta-N-acetylhexosaminidase (Am2136) from Akkermansia muciniphila [Akkermansia muciniphila ATCC BAA-835]
4A41_A 1.00e-48 1125 1262 23 159
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]
2V72_A 5.44e-30 1124 1264 8 143
Thestructure of the family 32 CBM from C. perfringens NanJ in complex with galactose [Clostridium perfringens]
4H04_A 6.30e-26 441 923 34 490
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]
2J7M_A 3.48e-23 1131 1263 10 148
Characterizationof a Family 32 CBM [Clostridium perfringens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B2UPR7 3.89e-140 353 1114 24 753
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
P0DTR4 2.40e-25 1125 1272 507 653
A type blood N-acetyl-alpha-D-galactosamine deacetylase OS=Flavonifractor plautii OX=292800 PE=1 SV=1
Q8XL08 6.40e-21 1123 1267 620 771
O-GlcNAcase NagJ OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=nagJ PE=1 SV=1
Q0TR53 6.40e-21 1123 1267 620 771
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
E8MGH9 4.37e-16 1137 1475 1520 1871
Beta-L-arabinobiosidase OS=Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b) OX=565042 GN=hypBA2 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
0.000314 0.998861 0.000291 0.000171 0.000169 0.000146

TMHMM  Annotations      download full data without filtering help

start end
12 29
1590 1609