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CAZyme Information: MGYG000000886_00492

You are here: Home > Sequence: MGYG000000886_00492

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 UBA2882 sp900542015
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; UBA2882; UBA2882 sp900542015
CAZyme ID MGYG000000886_00492
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1541 MGYG000000886_2|CGC3 164050.37 5.9262
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000886 2937871 MAG Denmark Europe
Gene Location Start: 121695;  End: 126320  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000886_00492.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 1408 1537 1e-15 0.9609375

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 2.74e-44 252 453 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 1.27e-36 253 452 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 2.28e-34 221 457 13 229
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam08481 GBS_Bsp-like 1.82e-27 873 958 2 88
GBS Bsp-like repeat. This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.
pfam08481 GBS_Bsp-like 2.23e-26 1072 1157 2 88
GBS Bsp-like repeat. This domain is found as a repeat in a number of Streptococcus proteins including some hypothetical proteins and Bsp. Bsp is a protein of group B Streptococcus (GBS) which might control cell morphology.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AEN97541.1 0.0 69 1539 129 1784
QRO35993.1 1.49e-316 69 1540 107 1764
QBF76227.1 1.49e-316 69 1540 107 1764
QEI32622.1 6.08e-249 3 1539 2 1310
QHB25110.1 6.08e-249 3 1539 2 1310

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1JWQ_A 1.08e-12 252 458 3 178
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5J72_A 1.71e-12 243 452 445 633
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]
7RAG_B 1.32e-09 253 460 19 213
ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]
4BIN_A 4.52e-07 251 462 174 399
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A 6.48e-07 248 455 2 223
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O51481 2.01e-21 1396 1505 67 169
Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
O48471 1.32e-14 252 460 4 185
Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
Q02114 3.20e-13 253 455 322 494
N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
P37134 2.91e-12 251 460 2 179
N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM PE=3 SV=1
P36548 1.76e-09 242 455 42 275
N-acetylmuramoyl-L-alanine amidase AmiA OS=Escherichia coli (strain K12) OX=83333 GN=amiA 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
0.000339 0.998855 0.000191 0.000226 0.000199 0.000173

TMHMM  Annotations      download full data without filtering help

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