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CAZyme Information: MGYG000001457_04196

You are here: Home > Sequence: MGYG000001457_04196

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 Pseudomonas_B luteola
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; Pseudomonadaceae; Pseudomonas_B; Pseudomonas_B luteola
CAZyme ID MGYG000001457_04196
CAZy Family CBM50
CAZyme Description N-acetylmuramoyl-L-alanine amidase AmiC
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
399 MGYG000001457_2|CGC4 42915.18 10.7363
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001457 5659210 Isolate not provided not provided
Gene Location Start: 167206;  End: 168405  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001457_04196.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10319 PRK10319 2.26e-73 136 381 36 277
N-acetylmuramoyl-L-alanine amidase AmiA.
COG0860 AmiC 1.02e-66 100 383 1 231
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
PRK10431 PRK10431 2.52e-59 8 384 7 420
N-acetylmuramoyl-l-alanine amidase II; Provisional
cd02696 MurNAc-LAA 1.17e-56 159 376 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 4.05e-47 160 376 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCA31092.1 1.85e-113 13 396 11 414
QZX82628.1 2.09e-113 13 396 15 418
BBT19073.1 2.36e-113 13 396 19 422
AYF89778.1 2.87e-113 13 391 15 413
BAN50917.1 2.23e-111 13 391 11 408

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BIN_A 4.76e-72 23 381 16 394
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A 1.51e-34 160 386 7 230
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A 1.99e-18 158 382 5 180
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4RN7_A 2.16e-17 160 383 6 185
ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
1JWQ_A 7.16e-13 159 379 3 175
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P63883 3.16e-73 1 381 8 408
N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli (strain K12) OX=83333 GN=amiC PE=1 SV=1
P63884 3.16e-73 1 381 8 408
N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=amiC PE=3 SV=1
Q9K0V3 1.85e-59 12 381 14 409
N-acetylmuramoyl-L-alanine amidase AmiC OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=amiC PE=1 SV=1
P36548 3.67e-55 140 380 40 276
N-acetylmuramoyl-L-alanine amidase AmiA OS=Escherichia coli (strain K12) OX=83333 GN=amiA PE=1 SV=1
P33772 4.35e-53 140 380 40 276
N-acetylmuramoyl-L-alanine amidase AmiA OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as TAT

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000007 0.000635 0.000002 0.999301 0.000045 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001457_04196.