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CAZyme Information: MGYG000001374_02583

You are here: Home > Sequence: MGYG000001374_02583

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 Mediterraneibacter torques
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Mediterraneibacter; Mediterraneibacter torques
CAZyme ID MGYG000001374_02583
CAZy Family CBM13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1540 MGYG000001374_5|CGC3 168962.15 5.1149
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001374 3092406 Isolate not provided not provided
Gene Location Start: 127537;  End: 132159  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001374_02583.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM13 1223 1377 1.7e-25 0.7819148936170213
CBM13 785 919 5.4e-22 0.7074468085106383
GH73 1406 1533 1.9e-20 0.9453125
CBM13 1076 1218 2.4e-20 0.7180851063829787
CBM13 929 1074 3.6e-20 0.7340425531914894

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02696 MurNAc-LAA 7.01e-32 274 475 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.
pfam14200 RicinB_lectin_2 3.23e-27 1260 1346 2 89
Ricin-type beta-trefoil lectin domain-like.
pfam01520 Amidase_3 4.75e-25 275 474 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 4.77e-24 268 481 38 231
N-acetylmuramoyl-L-alanine amidase [Cell wall/membrane/envelope biogenesis].
pfam14200 RicinB_lectin_2 6.57e-22 817 903 2 89
Ricin-type beta-trefoil lectin domain-like.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QRT50579.1 2.59e-242 116 1537 119 1696
VCV20908.1 3.06e-98 100 1532 169 1459
CBL13779.1 1.72e-97 100 1532 164 1454
CBL07763.1 2.42e-96 100 1532 163 1453
QRO35993.1 7.91e-90 71 1530 77 1756

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3PG0_A 5.77e-09 684 730 23 69
Crystalstructure of designed 3-fold symmetric protein, ThreeFoil [synthetic construct]
4BIN_A 2.77e-08 273 477 174 392
Crystalstructure of the E. coli N-acetylmuramoyl-L-alanine amidase AmiC [Escherichia coli K-12]
1JWQ_A 8.66e-08 274 379 3 103
Structureof the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus [Paenibacillus polymyxa]
5B2H_A 5.81e-06 694 970 18 278
Crystalstructure of HA33 from Clostridium botulinum serotype C strain Yoichi [Clostridium botulinum],5B2H_B Crystal structure of HA33 from Clostridium botulinum serotype C strain Yoichi [Clostridium botulinum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O51481 4.98e-25 1409 1540 75 198
Uncharacterized protein BB_0531 OS=Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) OX=224326 GN=BB_0531 PE=3 SV=1
Q06320 5.94e-11 273 482 2 179
Sporulation-specific N-acetylmuramoyl-L-alanine amidase OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlC PE=1 SV=1
P54525 6.70e-08 258 477 16 203
Uncharacterized protein YqiI OS=Bacillus subtilis (strain 168) OX=224308 GN=yqiI PE=3 SV=3
P63883 1.59e-07 273 477 188 406
N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli (strain K12) OX=83333 GN=amiC PE=1 SV=1
P63884 1.59e-07 273 477 188 406
N-acetylmuramoyl-L-alanine amidase AmiC OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) OX=199310 GN=amiC 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
0.003683 0.959884 0.035543 0.000311 0.000293 0.000255

TMHMM  Annotations      download full data without filtering help

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