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CAZyme Information: MGYG000002283_02412

You are here: Home > Sequence: MGYG000002283_02412

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 Bacillus_A paranthracis
Lineage Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A paranthracis
CAZyme ID MGYG000002283_02412
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
575 MGYG000002283_1|CGC18 64028.84 6.0877
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002283 5102264 Isolate China Asia
Gene Location Start: 2327274;  End: 2329001  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002283_02412.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG5632 CwlA 3.06e-37 230 391 1 165
N-acetylmuramoyl-L-alanine amidase CwlA [Cell wall/membrane/envelope biogenesis].
cd06583 PGRP 3.91e-27 252 378 1 126
Peptidoglycan recognition proteins (PGRPs) are pattern recognition receptors that bind, and in certain cases, hydrolyze peptidoglycans (PGNs) of bacterial cell walls. PGRPs have been divided into three classes: short PGRPs (PGRP-S), that are small (20 kDa) extracellular proteins; intermediate PGRPs (PGRP-I) that are 40-45 kDa and are predicted to be transmembrane proteins; and long PGRPs (PGRP-L), up to 90 kDa, which may be either intracellular or transmembrane. Several structures of PGRPs are known in insects and mammals, some bound with substrates like Muramyl Tripeptide (MTP) or Tracheal Cytotoxin (TCT). The substrate binding site is conserved in PGRP-LCx, PGRP-LE, and PGRP-Ialpha proteins. This family includes Zn-dependent N-Acetylmuramoyl-L-alanine Amidase, EC:3.5.1.28. This enzyme cleaves the amide bond between N-acetylmuramoyl and L-amino acids, preferentially D-lactyl-L-Ala, in bacterial cell walls. The structure for the bacteriophage T7 lysozyme shows that two of the conserved histidines and a cysteine are zinc binding residues. Site-directed mutagenesis of T7 lysozyme indicates that two conserved residues, a Tyr and a Lys, are important for amidase activity.
pfam01510 Amidase_2 1.51e-24 252 375 1 119
N-acetylmuramoyl-L-alanine amidase. This family includes zinc amidases that have N-acetylmuramoyl-L-alanine amidase activity EC:3.5.1.28. This enzyme domain cleaves the amide bond between N-acetylmuramoyl and L-amino acids in bacterial cell walls (preferentially: D-lactyl-L-Ala). The structure is known for the bacteriophage T7 structure and shows that two of the conserved histidines are zinc binding.
smart00644 Ami_2 2.70e-22 251 375 1 126
Ami_2 domain.
NF033190 inl_like_NEAT_1 2.25e-12 400 570 583 753
NEAT domain-containing leucine-rich repeat protein. Members of this family have an N-terminal NEAT (near transporter) domain often associated with iron transport, followed by a leucine-rich repeat region with significant sequence similarity to the internalins of Listeria monocytogenes. However, since Bacillus cereus (from which this protein was described, in PMID:16978259) is not considered an intracellular pathogen, and the function may be iron transport rather than internalization, applying the name "internalin" to this family probably would be misleading.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QTR69063.1 7.97e-248 1 575 1 591
QTR76806.1 7.97e-248 1 575 1 591
QTR85044.1 1.60e-247 1 575 1 591
QTR73010.1 1.60e-247 1 575 1 591
QTR89055.1 1.60e-247 1 575 1 591

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3HMB_A 4.00e-49 231 390 5 155
ChainA, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis],3HMB_B Chain B, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis],3HMB_C Chain C, N-acetylmuramoyl-L-alanine amidase xlyA [Bacillus subtilis]
3RDR_A 5.82e-47 238 390 12 155
Structureof the catalytic domain of XlyA [Bacillus subtilis]
1YB0_A 7.86e-31 234 392 5 155
Structureof PlyL [Bacillus anthracis],1YB0_B Structure of PlyL [Bacillus anthracis],1YB0_C Structure of PlyL [Bacillus anthracis]
2L47_A 9.33e-31 233 392 3 155
Solutionstructure of the PlyG catalytic domain [Bacillus phage Gamma]
2AR3_A 5.44e-30 234 392 5 155
ChainA, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis],2AR3_B Chain B, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis],2AR3_C Chain C, prophage lambdaba02, n-acetylmuramoyl-l-alanine amidase, family 2 [Bacillus anthracis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P54450 1.91e-46 231 390 2 153
N-acetylmuramoyl-L-alanine amidase CwlH OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlH PE=1 SV=1
P39800 1.87e-44 238 390 9 152
N-acetylmuramoyl-L-alanine amidase XlyA OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyA PE=1 SV=1
P14892 4.39e-28 233 379 3 143
N-acetylmuramoyl-L-alanine amidase CwlA OS=Bacillus sp. OX=1409 GN=cwlA PE=3 SV=1
O34391 6.20e-27 231 385 3 151
N-acetylmuramoyl-L-alanine amidase XlyB OS=Bacillus subtilis (strain 168) OX=224308 GN=xlyB PE=3 SV=1
P24808 2.18e-26 237 384 9 150
N-acetylmuramoyl-L-alanine amidase CwlA OS=Bacillus subtilis (strain 168) OX=224308 GN=cwlA PE=1 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
0.000304 0.998932 0.000202 0.000183 0.000177 0.000159

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002283_02412.