logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000050_01030

You are here: Home > Sequence: MGYG000000050_01030

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 Blautia_A sp900066505
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A sp900066505
CAZyme ID MGYG000000050_01030
CAZy Family GH73
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
495 MGYG000000050_7|CGC1 54086.83 6.821
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000050 3884369 Isolate United Kingdom Europe
Gene Location Start: 119458;  End: 120945  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000050_01030.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH73 230 361 1.1e-16 0.96875

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 1.43e-22 4 185 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 5.01e-22 5 184 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 6.34e-17 1 189 41 229
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam01832 Glucosaminidase 1.00e-08 232 311 2 91
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase. This family includes Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase EC:3.2.1.96. As well as the flageller protein J that has been shown to hydrolyze peptidoglycan.
smart00646 Ami_3 1.71e-05 66 184 4 113
Ami_3 domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUO23193.1 2.19e-199 202 495 1 294
ADL53623.1 1.03e-152 193 495 190 488
AFC63685.1 6.81e-151 185 495 189 498
QMW80001.1 1.15e-113 199 495 173 501
QIB57222.1 1.15e-113 199 495 173 501

PDB Hits      help

has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O51481 1.09e-21 193 359 33 192
Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000056 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000050_01030.