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CAZyme Information: MGYG000001958_01362

You are here: Home > Sequence: MGYG000001958_01362

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Intestinimonas;
CAZyme ID MGYG000001958_01362
CAZy Family GH3
CAZyme Description Beta-hexosaminidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
392 41568.7 4.0414
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001958 1726878 MAG Denmark Europe
Gene Location Start: 194;  End: 1372  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001958_01362.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH3 124 350 4.5e-45 0.9675925925925926

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam00933 Glyco_hydro_3 2.00e-66 65 384 1 315
Glycosyl hydrolase family 3 N terminal domain.
COG1472 BglX 6.40e-62 64 392 1 318
Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism].
PRK05337 PRK05337 2.14e-31 93 349 27 277
beta-hexosaminidase; Provisional
PRK15098 PRK15098 8.86e-21 57 391 38 358
beta-glucosidase BglX.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QCI59548.1 1.62e-275 1 392 1 392
BCK84132.1 9.22e-178 1 392 1 396
QUO36703.1 1.70e-174 39 392 37 398
QNL44190.1 3.17e-174 1 392 1 383
BAL01846.1 3.90e-155 1 392 1 403

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6K5J_A 1.73e-42 63 387 10 338
Structureof a glycoside hydrolase family 3 beta-N-acetylglucosaminidase from Paenibacillus sp. str. FPU-7 [Paenibacillaceae]
5BU9_A 2.07e-36 62 386 3 337
Crystalstructure of Beta-N-acetylhexosaminidase from Beutenbergia cavernae DSM 12333 [Beutenbergia cavernae DSM 12333],5BU9_B Crystal structure of Beta-N-acetylhexosaminidase from Beutenbergia cavernae DSM 12333 [Beutenbergia cavernae DSM 12333]
4YYF_A 4.77e-36 61 381 36 354
ChainA, Beta-N-acetylhexosaminidase [Mycolicibacterium smegmatis MC2 155],4YYF_B Chain B, Beta-N-acetylhexosaminidase [Mycolicibacterium smegmatis MC2 155],4YYF_C Chain C, Beta-N-acetylhexosaminidase [Mycolicibacterium smegmatis MC2 155]
6GFV_A 5.94e-35 62 386 14 337
Mtuberculosis LpqI [Mycobacterium tuberculosis H37Rv],6GFV_B M tuberculosis LpqI [Mycobacterium tuberculosis H37Rv]
4ZM6_A 6.22e-33 66 386 9 337
Aunique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain GH3 beta-N-acetylglucosaminidase [Rhizomucor miehei CAU432],4ZM6_B A unique GCN5-related glucosamine N-acetyltransferase region exist in the fungal multi-domain GH3 beta-N-acetylglucosaminidase [Rhizomucor miehei CAU432]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
L7N6B0 1.51e-35 3 386 5 380
Beta-hexosaminidase LpqI OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=lpqI PE=1 SV=1
A0A0H3M1P5 4.02e-35 3 386 5 380
Beta-hexosaminidase LpqI OS=Mycobacterium bovis (strain BCG / Pasteur 1173P2) OX=410289 GN=lpqI PE=3 SV=1
P40406 2.48e-31 54 391 32 398
Beta-hexosaminidase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagZ PE=1 SV=1
B2FPW9 1.11e-25 92 371 24 296
Beta-hexosaminidase OS=Stenotrophomonas maltophilia (strain K279a) OX=522373 GN=nagZ PE=3 SV=1
B4SRK3 1.11e-25 92 371 24 296
Beta-hexosaminidase OS=Stenotrophomonas maltophilia (strain R551-3) OX=391008 GN=nagZ PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000000 1.000063 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001958_01362.