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CAZyme Information: MGYG000000467_00289

You are here: Home > Sequence: MGYG000000467_00289

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 CAAGED01 sp900768505
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; CAAGED01; CAAGED01 sp900768505
CAZyme ID MGYG000000467_00289
CAZy Family GH20
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
492 MGYG000000467_4|CGC1 56872.16 6.4151
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000467 2445290 MAG Fiji Oceania
Gene Location Start: 31835;  End: 33313  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000467_00289.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH20 148 395 3.2e-29 0.6735905044510386

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06565 GH20_GcnA-like 1.99e-30 152 454 19 294
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 2.35e-16 77 328 206 491
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism].
cd02742 GH20_hexosaminidase 2.63e-14 148 393 14 232
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.
cd06564 GH20_DspB_LnbB-like 3.27e-14 137 392 3 239
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 1.01e-12 192 329 77 225
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
BBD46391.1 1.26e-144 6 489 53 528
ASV74378.1 1.03e-62 123 423 238 535
AQS53998.1 1.15e-28 165 434 37 313
QNN21342.1 3.78e-28 138 422 28 311
ALS28056.1 4.18e-27 137 440 5 314

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6YHH_A 3.76e-13 58 327 71 370
X-rayStructure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101],6YHH_B X-ray Structure of Flavobacterium johnsoniae chitobiase (FjGH20) [Flavobacterium johnsoniae UW101]
4PYS_A 8.63e-12 73 327 74 345
Thecrystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343],4PYS_B The crystal structure of beta-N-acetylhexosaminidase from Bacteroides fragilis NCTC 9343 [Bacteroides fragilis NCTC 9343]
6Q63_A 1.01e-09 77 304 106 356
BT0459[Bacteroides thetaiotaomicron],6Q63_B BT0459 [Bacteroides thetaiotaomicron],6Q63_C BT0459 [Bacteroides thetaiotaomicron]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P49008 1.21e-11 74 327 108 388
Beta-hexosaminidase OS=Porphyromonas gingivalis (strain ATCC BAA-308 / W83) OX=242619 GN=nahA PE=3 SV=2
Q7WUL4 2.98e-08 76 283 81 298
Beta-N-acetylhexosaminidase OS=Cellulomonas fimi OX=1708 GN=hex20 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
1.000054 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000467_00289.