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CAZyme Information: MGYG000001553_02455

You are here: Home > Sequence: MGYG000001553_02455

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 Clostridium_P mediterraneense
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium_P; Clostridium_P mediterraneense
CAZyme ID MGYG000001553_02455
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
915 MGYG000001553_5|CGC18 102049.5 8.4078
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001553 3045114 Isolate not provided not provided
Gene Location Start: 2187920;  End: 2190667  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001553_02455.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd06583 PGRP 1.74e-26 766 892 2 124
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 2.44e-25 766 893 2 121
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.
smart00701 PGRP 2.66e-16 759 879 21 135
Animal peptidoglycan recognition proteins homologous to Bacteriophage T3 lysozyme. The bacteriophage molecule, but not its moth homologue, has been shown to have N-acetylmuramoyl-L-alanine amidase activity. One member of this family, Tag7, is a cytokine.
smart00644 Ami_2 7.55e-12 765 891 2 126
Ami_2 domain.
PHA00447 PHA00447 6.43e-10 767 892 11 131
lysozyme

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AYE34895.1 4.01e-163 27 744 34 778
QAS60290.1 5.95e-162 27 744 34 778
QLY79091.1 4.96e-127 195 744 38 586
AGK97878.1 1.05e-109 200 741 38 591
ADL53568.1 1.91e-93 184 740 122 699

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6SRT_A 5.69e-27 766 904 41 166
EndolysineN-acetylmuramoyl-L-alanine amidase LysCS from Clostridium intestinale URNW [Clostridium intestinale URNW]
6SSC_A 1.07e-26 766 904 64 189
N-acetylmuramoyl-L-alanineamidase LysC from Clostridium intestinale URNW [Clostridium intestinale]
7F5I_A 2.22e-17 764 900 29 152
ChainA, amidase [Clostridium perfringens str. 13]
4Z8I_A 6.59e-11 768 902 89 221
Crystalstructure of Branchiostoma belcheri tsingtauense peptidoglycan recognition protein 3 [Branchiostoma belcheri tsingtauense]
4ZXM_A 8.73e-11 768 902 118 250
Crystalstructure of PGRP domain from Branchiostoma belcheri tsingtauense peptidoglycan recognition protein 3 [Branchiostoma belcheri tsingtauense]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9V4X2 1.26e-11 762 894 40 171
Peptidoglycan-recognition protein SC2 OS=Drosophila melanogaster OX=7227 GN=PGRP-SC2 PE=2 SV=1
Q70PU1 3.15e-11 770 894 48 171
Peptidoglycan-recognition protein SC2 OS=Drosophila simulans OX=7240 GN=PGRP-SC2 PE=3 SV=1
C0HK99 5.93e-11 762 892 41 170
Peptidoglycan-recognition protein SC1b OS=Drosophila melanogaster OX=7227 GN=PGRP-SC1b PE=1 SV=1
C0HK98 5.93e-11 762 892 41 170
Peptidoglycan-recognition protein SC1a OS=Drosophila melanogaster OX=7227 GN=PGRP-SC1a PE=3 SV=1
Q70PU2 6.80e-10 762 892 41 170
Peptidoglycan-recognition protein SC1a/b OS=Drosophila simulans OX=7240 GN=PGRP-SC1a PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000281 0.999025 0.000186 0.000171 0.000158 0.000153

TMHMM  Annotations      download full data without filtering help

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