logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000002436_04531

You are here: Home > Sequence: MGYG000002436_04531

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 Pigmentiphaga sp002188635
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Pigmentiphaga; Pigmentiphaga sp002188635
CAZyme ID MGYG000002436_04531
CAZy Family CBM50
CAZyme Description N-acetylmuramoyl-L-alanine amidase AmiC
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
476 MGYG000002436_43|CGC4 51411.81 7.6395
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002436 5862145 Isolate Canada North America
Gene Location Start: 142792;  End: 144222  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002436_04531.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10319 PRK10319 6.81e-73 220 464 42 276
N-acetylmuramoyl-L-alanine amidase AmiA.
COG0860 AmiC 4.69e-62 238 467 37 231
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
cd02696 MurNAc-LAA 2.36e-59 245 461 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.
PRK10431 PRK10431 2.39e-57 93 468 51 420
N-acetylmuramoyl-l-alanine amidase II; Provisional
pfam01520 Amidase_3 8.88e-51 246 460 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
AXY42113.1 1.07e-109 44 469 5 417
QJQ99761.1 8.53e-109 44 469 5 417
APX92538.1 1.09e-107 56 469 12 410
QHD51572.1 9.96e-107 62 469 27 426
BCA92323.1 4.20e-106 43 469 9 428

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BIN_A 2.42e-123 65 472 21 401
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
3NE8_A 5.32e-36 246 463 7 223
Thecrystal structure of a domain from N-acetylmuramoyl-l-alanine amidase of Bartonella henselae str. Houston-1 [Bartonella henselae]
5EMI_A 4.82e-26 244 466 5 180
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
4RN7_A 9.63e-16 241 463 1 181
ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
1JWQ_A 5.07e-13 243 463 1 175
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 3.26e-124 39 472 8 415
N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli (strain K12) OX=83333 GN=amiC PE=1 SV=1
P63884 3.26e-124 39 472 8 415
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 1.57e-113 39 463 4 407
N-acetylmuramoyl-L-alanine amidase AmiC OS=Neisseria meningitidis serogroup B (strain MC58) OX=122586 GN=amiC PE=1 SV=1
P33772 1.85e-58 246 464 59 276
N-acetylmuramoyl-L-alanine amidase AmiA OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amiA PE=3 SV=1
P36548 2.60e-58 246 464 59 276
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 TAT

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.005128 0.014119 0.000411 0.911248 0.069078 0.000008

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002436_04531.