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CAZyme Information: MGYG000004714_01079

You are here: Home > Sequence: MGYG000004714_01079

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; Clostridiales; Clostridiaceae; Clostridium_X;
CAZyme ID MGYG000004714_01079
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1189 129622.77 6.1585
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004714 2587994 MAG China Asia
Gene Location Start: 62;  End: 3631  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004714_01079.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0791 Spr 4.36e-27 1056 1175 62 183
Cell wall-associated hydrolase, NlpC family [Cell wall/membrane/envelope biogenesis].
pfam00877 NLPC_P60 8.37e-27 1081 1179 1 96
NlpC/P60 family. The function of this domain is unknown. It is found in several lipoproteins.
cd06583 PGRP 1.50e-23 14 141 1 124
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.
NF033742 NlpC_p60_RipB 1.12e-22 1069 1179 73 196
NlpC/P60 family peptidoglycan endopeptidase RipB.
pfam01510 Amidase_2 6.89e-22 15 140 2 119
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQM60290.1 4.25e-119 416 1066 47 722
QLY80841.1 1.48e-109 2 809 56 930
SQI04537.1 1.32e-102 342 1103 119 914
BAB80937.1 7.72e-98 235 1103 23 909
ADA00360.1 7.72e-98 235 1103 23 909

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3HMB_A 2.30e-23 6 158 17 156
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]
7CFL_A 1.18e-22 1072 1188 17 138
ChainA, Putative cell wall hydrolase phosphatase-associated protein [Clostridioides difficile],7CFL_B Chain B, Putative cell wall hydrolase phosphatase-associated protein [Clostridioides difficile],7CFL_C Chain C, Putative cell wall hydrolase phosphatase-associated protein [Clostridioides difficile],7CFL_D Chain D, Putative cell wall hydrolase phosphatase-associated protein [Clostridioides difficile]
3RDR_A 2.74e-22 6 158 17 156
Structureof the catalytic domain of XlyA [Bacillus subtilis]
6B8C_A 1.06e-21 1066 1177 25 134
Crystalstructure of NlpC/p60 domain of peptidoglycan hydrolase SagA [Enterococcus faecium]
3H41_A 7.81e-15 1071 1188 191 310
CRYSTALSTRUCTURE OF A NLPC/P60 FAMILY PROTEIN (BCE_2878) FROM BACILLUS CEREUS ATCC 10987 AT 1.79 A RESOLUTION [Bacillus cereus ATCC 10987]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O32041 1.20e-22 654 968 26 312
Putative N-acetylmuramoyl-L-alanine amidase YrvJ OS=Bacillus subtilis (strain 168) OX=224308 GN=yrvJ PE=3 SV=1
P39800 4.62e-21 6 163 14 158
N-acetylmuramoyl-L-alanine amidase XlyA OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyA PE=1 SV=1
P54450 1.70e-19 10 165 18 161
N-acetylmuramoyl-L-alanine amidase CwlH OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlH PE=1 SV=1
P13692 3.16e-17 1066 1177 399 508
Protein P54 OS=Enterococcus faecium OX=1352 PE=3 SV=2
O35010 2.22e-16 1062 1174 166 278
Gamma-D-glutamyl-L-lysine dipeptidyl-peptidase OS=Bacillus subtilis (strain 168) OX=224308 GN=ykfC PE=1 SV=2

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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004714_01079.