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CAZyme Information: MGYG000000902_04127

You are here: Home > Sequence: MGYG000000902_04127

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 neonatale
Lineage Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium neonatale
CAZyme ID MGYG000000902_04127
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
422 MGYG000000902_111|CGC1 45821.41 6.4228
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000902 4770522 MAG China Asia
Gene Location Start: 2190;  End: 3458  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000902_04127.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 6.57e-58 225 418 1 172
N-acetylmuramoyl-L-alanine amidase or MurNAc-LAA (also known as peptidoglycan aminohydrolase, NAMLA amidase, NAMLAA, Amidase 3, and peptidoglycan amidase; EC 3.5.1.28) is an autolysin that hydrolyzes the amide bond between N-acetylmuramoyl and L-amino acids in certain cell wall glycopeptides. These proteins are Zn-dependent peptidases with highly conserved residues involved in cation co-ordination. MurNAc-LAA in this family is one of several peptidoglycan hydrolases (PGHs) found in bacterial and bacteriophage or prophage genomes that are involved in the degradation of the peptidoglycan. In Escherichia coli, there are five MurNAc-LAAs present: AmiA, AmiB, AmiC and AmiD that are periplasmic, and AmpD that is cytoplasmic. Three of these (AmiA, AmiB and AmiC) belong to this family, the other two (AmiD and AmpD) do not. E. coli AmiA, AmiB and AmiC play an important role in cleaving the septum to release daughter cells after cell division. In general, bacterial MurNAc-LAAs are members of the bacterial autolytic system and carry a signal peptide in their N-termini that allows their transport across the cytoplasmic membrane. However, the bacteriophage MurNAc-LAAs are endolysins since these phage-encoded enzymes break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle. As opposed to autolysins, almost all endolysins have no signal peptides and their translocation through the cytoplasmic membrane is thought to proceed with the help of phage-encoded holin proteins. The amidase catalytic module is fused to another functional module (cell wall binding module or CWBM) either at the N- or C-terminus, which is responsible for high affinity binding of the protein to the cell wall.
pfam01520 Amidase_3 2.72e-49 226 417 1 172
N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
COG0860 AmiC 1.29e-44 210 419 29 226
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
smart00646 Ami_3 5.06e-22 297 417 3 113
Ami_3 domain.
PRK10319 PRK10319 6.16e-11 204 417 37 272
N-acetylmuramoyl-L-alanine amidase AmiA.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AOR24546.1 9.65e-113 37 421 25 623
QUF83267.1 1.43e-108 38 420 26 608
QCJ04078.1 3.16e-107 38 420 26 608
ANF15512.1 3.16e-107 38 420 26 608
AOR95460.1 3.16e-107 38 420 26 608

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5J72_A 5.74e-20 222 422 450 638
ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630]
7RAG_B 1.20e-19 220 413 13 201
ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]
4RN7_A 3.09e-19 225 421 5 182
ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
1JWQ_A 1.21e-18 224 421 2 176
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5EMI_A 1.37e-16 223 421 4 178
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54525 1.34e-22 217 417 23 200
Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q02114 2.09e-20 212 415 308 489
N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
Q8CP02 4.18e-14 214 419 110 287
Probable cell wall amidase LytH OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=lytH PE=3 SV=1
Q5HNS0 5.64e-14 214 419 110 287
Probable cell wall amidase LytH OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=lytH PE=3 SV=1
P50864 9.00e-14 209 413 26 221
Germination-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlD PE=1 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
0.000278 0.999088 0.000164 0.000180 0.000157 0.000139

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000902_04127.