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CAZyme Information: MGYG000001708_00589

You are here: Home > Sequence: MGYG000001708_00589

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 rustigianii
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Providencia; Providencia rustigianii
CAZyme ID MGYG000001708_00589
CAZy Family CBM50
CAZyme Description N-acetylmuramoyl-L-alanine amidase AmiB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
438 47142.78 10.2954
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001708 3896203 Isolate not provided not provided
Gene Location Start: 77215;  End: 78531  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001708_00589.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10431 PRK10431 0.0 22 438 9 426
N-acetylmuramoyl-l-alanine amidase II; Provisional
COG0860 AmiC 4.70e-78 175 431 8 231
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696 MurNAc-LAA 7.12e-66 207 424 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 6.52e-59 208 424 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 1.15e-57 160 428 23 276
N-acetylmuramoyl-L-alanine amidase AmiA.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ANI30689.1 2.83e-153 33 438 24 428
AUX94894.1 4.52e-152 28 438 15 417
AJI94315.1 7.11e-152 33 438 12 416
CEK26170.1 3.92e-151 33 438 25 426
QTD75272.1 3.92e-151 33 438 25 426

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BIN_A 2.57e-44 63 428 46 393
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A 7.51e-29 208 427 7 223
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A 3.14e-20 202 427 1 177
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
1JWQ_A 1.83e-18 207 427 3 175
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A 1.30e-16 208 427 6 181
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 1.29e-136 35 438 22 426
N-acetylmuramoyl-L-alanine amidase AmiB OS=Escherichia coli (strain K12) OX=83333 GN=amiB PE=1 SV=2
P26366 2.43e-135 22 438 9 420
N-acetylmuramoyl-L-alanine amidase AmiB OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiB PE=3 SV=2
P44493 1.64e-82 206 424 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 7.06e-53 203 428 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 1.35e-49 206 429 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
0.000591 0.998644 0.000240 0.000184 0.000160 0.000149

TMHMM  Annotations      download full data without filtering help

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