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CAZyme Information: MGYG000004295_01177

You are here: Home > Sequence: MGYG000004295_01177

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 Providencia rettgeri
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Providencia; Providencia rettgeri
CAZyme ID MGYG000004295_01177
CAZy Family CBM50
CAZyme Description N-acetylmuramoyl-L-alanine amidase AmiB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
428 46483.16 10.25
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004295 4142275 MAG Israel Asia
Gene Location Start: 44384;  End: 45670  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004295_01177.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10431 PRK10431 0.0 22 428 9 426
N-acetylmuramoyl-l-alanine amidase II; Provisional
COG0860 AmiC 1.92e-76 190 421 37 231
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696 MurNAc-LAA 6.81e-66 197 414 1 171
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 1.62e-59 198 414 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.
PRK10319 PRK10319 1.14e-57 160 418 27 276
N-acetylmuramoyl-L-alanine amidase AmiA.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AHF78500.1 9.30e-157 28 428 15 429
ANI30689.1 3.76e-156 28 428 19 428
AJI94315.1 4.70e-155 28 428 7 416
AKF39858.1 1.18e-154 35 428 15 446
ALG43566.1 1.18e-154 35 428 15 446

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BIN_A 9.25e-50 63 418 46 393
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A 1.31e-30 198 417 7 223
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A 4.69e-22 192 417 1 177
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
1JWQ_A 4.43e-18 197 417 3 175
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A 2.75e-15 193 417 1 181
ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26365 4.25e-140 22 428 9 426
N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2
P26366 1.61e-138 28 428 15 420
N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P44493 9.05e-79 196 414 23 243
Probable N-acetylmuramoyl-L-alanine amidase AmiB OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=amiB PE=3 SV=1
P57638 3.95e-53 193 418 2 228
Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) OX=107806 GN=amiB PE=3 SV=1
Q89A33 5.88e-49 196 419 1 210
Putative N-acetylmuramoyl-L-alanine amidase OS=Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp) OX=224915 GN=amiB 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
0.038270 0.958507 0.002261 0.000397 0.000276 0.000257

TMHMM  Annotations      download full data without filtering help

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