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CAZyme Information: MGYG000003699_00485

You are here: Home > Sequence: MGYG000003699_00485

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 Holdemanella sp003436425
Lineage Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelotrichaceae; Holdemanella; Holdemanella sp003436425
CAZyme ID MGYG000003699_00485
CAZy Family CBM13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1125 123966.71 5.1351
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003699 2572738 Isolate China Asia
Gene Location Start: 39300;  End: 42677  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003699_00485.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM13 636 779 9.1e-23 0.7180851063829787
CBM13 795 947 5.2e-21 0.776595744680851
CBM13 477 628 9e-21 0.7659574468085106
GH73 993 1120 2.7e-17 0.953125

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 4.14e-52 249 450 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 7.29e-47 250 449 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 5.86e-41 225 456 19 231
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
TIGR02883 spore_cwlD 2.10e-28 249 427 2 165
N-acetylmuramoyl-L-alanine amidase CwlD. Members of this protein family are the CwlD family of N-acetylmuramoyl-L-alanine amidase. This family has been called the germination-specific N-acetylmuramoyl-L-alanine amidase. CwlD is required, along with the putative deactylase PdaA, to make muramic delta-lactam, a novel peptidoglycan constituent found only in spores. CwlD mutants show a germination defect. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Sporulation and germination]
pfam14200 RicinB_lectin_2 1.96e-20 513 600 2 89
Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QEI32622.1 1.40e-67 88 1125 66 1312
QHB25110.1 1.40e-67 88 1125 66 1312
QRT31212.1 3.32e-67 82 1125 60 1312
CBL07763.1 6.10e-67 89 1122 164 1457
CBL13779.1 2.54e-66 89 1122 165 1458

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5J72_A 1.41e-17 207 449 411 633
ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630]
1JWQ_A 1.22e-13 250 384 4 128
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
4RN7_A 2.02e-13 249 453 5 182
ChainA, N-acetylmuramoyl-L-alanine amidase [Clostridioides difficile 630]
5EMI_A 1.67e-11 245 345 2 98
ChainA, Cell wall hydrolase/autolysin [Nostoc punctiforme PCC 73102]
7RAG_B 5.63e-09 249 427 18 184
ChainB, Germination-specific N-acetylmuramoyl-L-alanine amidase, Autolysin [Clostridioides difficile]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O51481 2.62e-21 989 1124 68 197
Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
O48471 1.01e-16 250 459 5 187
Endolysin OS=Bacillus phage SPP1 OX=10724 GN=25 PE=4 SV=1
P54525 2.66e-15 247 451 29 202
Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
Q02114 1.30e-14 228 430 299 473
N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
P37134 2.99e-11 250 462 4 184
N-acetylmuramoyl-L-alanine amidase CwlM OS=Bacillus licheniformis OX=1402 GN=cwlM 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
0.038215 0.808073 0.150697 0.001557 0.000794 0.000640

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003699_00485.