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CAZyme Information: MGYG000001177_01579

You are here: Home > Sequence: MGYG000001177_01579

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 Massilicoli timonensis
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Massilicoli; Massilicoli timonensis
CAZyme ID MGYG000001177_01579
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
336 MGYG000001177_33|CGC1 36405.81 7.6518
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001177 1850660 MAG Austria Europe
Gene Location Start: 144002;  End: 145012  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001177_01579.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06583 PGRP 3.30e-22 22 163 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 5.16e-17 21 163 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 3.12e-14 21 148 2 117
Ami_2 domain.
COG5632 CwlA 9.28e-05 2 149 7 141
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis].
pfam08239 SH3_3 6.35e-04 280 332 1 52
Bacterial SH3 domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AFC63685.1 1.84e-151 1 336 1 498
QBF75599.1 6.47e-116 1 336 174 499
AMP42248.1 1.92e-115 1 334 1 454
ADL53623.1 4.66e-113 1 215 1 216
QQQ98955.1 2.71e-110 1 187 1 191

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3HMB_A 2.36e-06 18 95 27 101
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 5.92e-06 20 95 29 101
Structureof the catalytic domain of XlyA [Bacillus subtilis]

Swiss-Prot Hits      help

has no Swissprot hit.

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
1.000036 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001177_01579.