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CAZyme Information: MGYG000002131_01282

You are here: Home > Sequence: MGYG000002131_01282

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 CAG-882 sp900545455
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; CAG-882; CAG-882 sp900545455
CAZyme ID MGYG000002131_01282
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
496 54827.07 8.0995
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002131 2861336 MAG United States North America
Gene Location Start: 10993;  End: 12483  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002131_01282.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 213 343 1.4e-18 0.9609375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01510 Amidase_2 7.49e-34 21 154 1 121
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.
cd06583 PGRP 1.77e-26 21 155 1 126
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.
COG3023 AmpD 9.37e-21 5 155 21 167
N-acetyl-anhydromuramyl-L-alanine amidase AmpD [Cell wall/membrane/envelope biogenesis].
smart00644 Ami_2 9.45e-19 20 152 1 126
Ami_2 domain.
COG5632 CwlA 1.18e-12 6 175 7 169
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QMW80001.1 3.54e-100 1 470 1 470
QIB57222.1 3.54e-100 1 470 1 470
AFC63685.1 2.01e-80 43 344 44 366
ADL53623.1 9.70e-78 25 358 25 373
QUO23193.1 9.12e-70 184 358 1 174

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1J3G_A 7.97e-09 51 178 73 185
ChainA, AmpD protein [Citrobacter freundii],2Y2B_A crystal structure of AmpD in complex with reaction products [Citrobacter freundii],2Y2B_B crystal structure of AmpD in complex with reaction products [Citrobacter freundii],2Y2B_C crystal structure of AmpD in complex with reaction products [Citrobacter freundii],2Y2C_A crystal structure of AmpD Apoenzyme [Citrobacter freundii],2Y2C_B crystal structure of AmpD Apoenzyme [Citrobacter freundii],2Y2C_C crystal structure of AmpD Apoenzyme [Citrobacter freundii],2Y2D_A crystal structure of AmpD holoenzyme [Citrobacter freundii],2Y2D_B crystal structure of AmpD holoenzyme [Citrobacter freundii],2Y2D_C crystal structure of AmpD holoenzyme [Citrobacter freundii],2Y2E_A crystal structure of AmpD grown at pH 5.5 [Citrobacter freundii],2Y2E_B crystal structure of AmpD grown at pH 5.5 [Citrobacter freundii],2Y2E_C crystal structure of AmpD grown at pH 5.5 [Citrobacter freundii]
2Y28_A 1.46e-08 51 178 73 185
crystalstructure of Se-Met AmpD derivative [Citrobacter freundii],2Y28_B crystal structure of Se-Met AmpD derivative [Citrobacter freundii],2Y28_C crystal structure of Se-Met AmpD derivative [Citrobacter freundii]
2BH7_A 3.66e-08 21 154 28 162
Crystalstructure of a SeMet derivative of AmiD at 2.2 angstroms [Escherichia coli K-12]
2WKX_A 3.66e-08 21 154 28 162
Crystalstructure of the native E. coli zinc amidase AmiD [Escherichia coli K-12],3D2Y_A Complex of the N-acetylmuramyl-L-alanine amidase AmiD from E.coli with the substrate anhydro-N-acetylmuramic acid-L-Ala-D-gamma-Glu-L-Lys [Escherichia coli str. K-12 substr. MG1655],3D2Z_A Complex of the N-acetylmuramyl-L-alanine amidase AmiD from E.coli with the product L-Ala-D-gamma-Glu-L-Lys [Escherichia coli str. K-12 substr. MG1655]
2L47_A 1.79e-06 19 153 20 139
Solutionstructure of the PlyG catalytic domain [Bacillus phage Gamma]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O51481 5.22e-24 192 346 50 197
Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
P36550 2.12e-11 20 156 22 156
N-acetylmuramoyl-L-alanine amidase CwlL OS=Bacillus licheniformis OX=1402 GN=cwlL PE=3 SV=1
Q99125 3.64e-11 50 156 57 155
Probable N-acetylmuramoyl-L-alanine amidase OS=Bacillus licheniformis OX=1402 PE=3 SV=1
P0CL03 1.54e-09 51 178 73 185
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=ampD PE=3 SV=1
E1W818 7.05e-09 51 178 73 185
1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD OS=Salmonella typhimurium (strain SL1344) OX=216597 GN=ampD PE=3 SV=1

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
0.997007 0.002533 0.000045 0.000017 0.000010 0.000406

TMHMM  Annotations      download full data without filtering help

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