Species | Mediterraneibacter sp900555215 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter sp900555215 | |||||||||||
CAZyme ID | MGYG000002596_02024 | |||||||||||
CAZy Family | GH3 | |||||||||||
CAZyme Description | Beta-hexosaminidase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 4516; End: 6489 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH3 | 148 | 379 | 2.4e-55 | 0.9814814814814815 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1472 | BglX | 3.69e-81 | 81 | 418 | 1 | 315 | Periplasmic beta-glucosidase and related glycosidases [Carbohydrate transport and metabolism]. |
pfam00933 | Glyco_hydro_3 | 1.20e-80 | 82 | 414 | 1 | 316 | Glycosyl hydrolase family 3 N terminal domain. |
cd02696 | MurNAc-LAA | 8.95e-51 | 452 | 652 | 1 | 172 | N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall. |
PRK05337 | PRK05337 | 1.45e-48 | 120 | 379 | 26 | 279 | beta-hexosaminidase; Provisional |
COG0860 | AmiC | 2.93e-44 | 408 | 657 | 3 | 230 | N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWY98601.1 | 4.16e-158 | 42 | 418 | 43 | 419 |
CBK77067.1 | 1.20e-128 | 73 | 425 | 151 | 501 |
CBL36844.1 | 2.40e-128 | 73 | 425 | 151 | 501 |
QJU16873.1 | 8.08e-124 | 70 | 417 | 91 | 438 |
ASU30242.1 | 9.03e-123 | 70 | 417 | 91 | 438 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6K5J_A | 6.05e-69 | 81 | 427 | 11 | 349 | Structureof a glycoside hydrolase family 3 beta-N-acetylglucosaminidase from Paenibacillus sp. str. FPU-7 [Paenibacillaceae] |
3BMX_A | 8.21e-68 | 77 | 417 | 38 | 395 | Beta-N-hexosaminidase(YbbD) from Bacillus subtilis [Bacillus subtilis],3BMX_B Beta-N-hexosaminidase (YbbD) from Bacillus subtilis [Bacillus subtilis],3NVD_A Structure of YBBD in complex with pugnac [Bacillus subtilis],3NVD_B Structure of YBBD in complex with pugnac [Bacillus subtilis] |
3LK6_A | 2.53e-67 | 77 | 417 | 12 | 369 | ChainA, Lipoprotein ybbD [Bacillus subtilis],3LK6_B Chain B, Lipoprotein ybbD [Bacillus subtilis],3LK6_C Chain C, Lipoprotein ybbD [Bacillus subtilis],3LK6_D Chain D, Lipoprotein ybbD [Bacillus subtilis] |
4GYJ_A | 4.72e-67 | 77 | 417 | 42 | 399 | Crystalstructure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1) [Bacillus subtilis subsp. subtilis str. 168],4GYJ_B Crystal structure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1) [Bacillus subtilis subsp. subtilis str. 168],4GYK_A Crystal structure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1211) [Bacillus subtilis subsp. subtilis str. 168],4GYK_B Crystal structure of mutant (D318N) bacillus subtilis family 3 glycoside hydrolase (nagz) in complex with glcnac-murnac (space group P1211) [Bacillus subtilis subsp. subtilis str. 168] |
4ZM6_A | 1.87e-46 | 79 | 415 | 5 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P40406 | 4.49e-67 | 77 | 417 | 38 | 395 | Beta-hexosaminidase OS=Bacillus subtilis (strain 168) OX=224308 GN=nagZ PE=1 SV=1 |
P48823 | 6.65e-50 | 115 | 418 | 59 | 383 | Beta-hexosaminidase A OS=Pseudoalteromonas piscicida OX=43662 GN=cht60 PE=1 SV=1 |
L7N6B0 | 3.34e-36 | 76 | 415 | 54 | 380 | Beta-hexosaminidase LpqI OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=lpqI PE=1 SV=1 |
A0A0H3M1P5 | 8.49e-36 | 76 | 415 | 54 | 380 | Beta-hexosaminidase LpqI OS=Mycobacterium bovis (strain BCG / Pasteur 1173P2) OX=410289 GN=lpqI PE=3 SV=1 |
Q31G32 | 1.16e-35 | 120 | 404 | 36 | 316 | Beta-hexosaminidase OS=Hydrogenovibrio crunogenus (strain DSM 25203 / XCL-2) OX=317025 GN=nagZ PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
0.567784 | 0.031705 | 0.399767 | 0.000170 | 0.000329 | 0.000251 |
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