Species | Anaerostipes sp000508985 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerostipes; Anaerostipes sp000508985 | |||||||||||
CAZyme ID | MGYG000000052_03281 | |||||||||||
CAZy Family | GH73 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 6190; End: 6723 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd06583 | PGRP | 8.65e-23 | 22 | 167 | 2 | 123 | Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity. |
pfam01510 | Amidase_2 | 1.45e-17 | 21 | 167 | 1 | 119 | N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding. |
smart00644 | Ami_2 | 1.65e-15 | 21 | 154 | 2 | 119 | Ami_2 domain. |
COG5632 | CwlA | 7.23e-10 | 2 | 153 | 7 | 141 | N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QQQ98955.1 | 2.95e-113 | 1 | 177 | 1 | 177 |
AFC63685.1 | 3.66e-113 | 1 | 177 | 1 | 177 |
QJU15163.1 | 4.25e-104 | 1 | 177 | 1 | 177 |
AMP42248.1 | 2.86e-102 | 1 | 177 | 1 | 177 |
ADL53623.1 | 1.59e-101 | 1 | 177 | 1 | 173 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3HMB_A | 4.34e-07 | 34 | 99 | 25 | 101 | ChainA, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis],3HMB_B Chain B, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis],3HMB_C Chain C, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis] |
3RDR_A | 8.28e-07 | 42 | 99 | 33 | 101 | Structureof the catalytic domain of XlyA [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P24808 | 2.34e-06 | 28 | 122 | 15 | 117 | N-acetylmuramoyl-L-alanine amidase CwlA OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlA PE=1 SV=1 |
P54450 | 2.91e-06 | 62 | 99 | 62 | 99 | N-acetylmuramoyl-L-alanine amidase CwlH OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlH PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000049 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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