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CAZyme Information: MGYG000003107_00745

You are here: Home > Sequence: MGYG000003107_00745

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 Collinsella sp900541245
Lineage Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp900541245
CAZyme ID MGYG000003107_00745
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1004 MGYG000003107_12|CGC1 107357.48 4.9417
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003107 2129463 MAG Spain Europe
Gene Location Start: 43453;  End: 46467  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003107_00745.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 879 1002 1.2e-16 0.9609375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 4.69e-49 185 387 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.
COG0860 AmiC 2.03e-43 177 392 36 230
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam01520 Amidase_3 4.14e-43 187 386 2 172
N-acetylmuramoyl-L-alanine amidase. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls.
PRK10431 PRK10431 6.15e-18 185 390 193 416
N-acetylmuramoyl-l-alanine amidase II; Provisional
smart00646 Ami_3 2.19e-17 253 386 1 113
Ami_3 domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VCV20908.1 9.85e-85 39 994 170 1444
QTU85010.1 3.59e-67 37 996 114 999
QEI32622.1 8.47e-65 39 999 67 1305
QHB25110.1 8.47e-65 39 999 67 1305
CBL07763.1 2.56e-64 39 819 164 986

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5EMI_A 5.95e-14 187 388 8 176
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
3NE8_A 2.36e-13 187 401 8 234
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5J72_A 4.26e-13 176 386 444 633
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]
1JWQ_A 2.26e-10 185 388 3 174
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4BIN_A 9.98e-10 178 291 168 266
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O51481 3.61e-24 875 986 68 179
Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
Q63870 5.28e-24 349 820 377 850
Collagen alpha-1(VII) chain OS=Mus musculus OX=10090 GN=Col7a1 PE=1 SV=3
O48471 4.37e-23 188 396 7 187
Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q02388 7.98e-23 365 820 390 849
Collagen alpha-1(VII) chain OS=Homo sapiens OX=9606 GN=COL7A1 PE=1 SV=2
P37134 3.85e-21 188 396 6 181
N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM 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
0.000302 0.998981 0.000218 0.000186 0.000162 0.000145

TMHMM  Annotations      download full data without filtering help

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