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CAZyme Information: MGYG000001576_01011

You are here: Home > Sequence: MGYG000001576_01011

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 Dysosmobacter sp014297375
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; Dysosmobacter; Dysosmobacter sp014297375
CAZyme ID MGYG000001576_01011
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
447 MGYG000001576_6|CGC1 46041.82 4.4036
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001576 3081635 MAG United States North America
Gene Location Start: 94602;  End: 95945  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001576_01011.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CBM50 403 446 1.8e-16 0.975

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd02252 nylC_like 2.80e-92 38 347 3 259
nylC-like family; composed of proteins with similarity to Flavobacterium endo-type 6-aminohexanoate-oligomer hydrolase (EIII), the product of the nylon oligomer degradation gene, nylC. EIII is an amide hydrolase that catalyzes the degradation of highly-polymerized 6-aminohexanoate oligomers. Together with other nylon degradation enzymes, such as 6-aminohexanoate cyclic dimer hydrolase (EI) and 6-aminohexanoate dimer hydrolase (EII), EIII plays a role in the detoxification and biological removal of the synthetic by-products of nylon manufacture. EIII shows sequence similarity to L-aminopeptidase D-amidase/D-esterase (DmpA), an aminopeptidase that releases N-terminal D and L amino acids from peptide substrates. Like DmpA, EIII undergoes autocatalytic cleavage in front of a nucleophile to form a heterodimer. DmpA shows similarity in catalytic mechanism to N-terminal nucleophile (Ntn) hydrolases, which are enzymes that catalyze the cleavage of amide bonds through the nucleophilic attack of the side chain of an N-terminal serine, threonine, or cysteine.
COG3191 DmpA 7.00e-68 38 363 19 339
L-aminopeptidase/D-esterase [Amino acid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism].
pfam03576 Peptidase_S58 4.57e-46 38 356 5 309
Peptidase family S58.
cd00118 LysM 3.42e-16 401 445 1 45
Lysin Motif is a small domain involved in binding peptidoglycan. LysM, a small globular domain with approximately 40 amino acids, is a widespread protein module involved in binding peptidoglycan in bacteria and chitin in eukaryotes. The domain was originally identified in enzymes that degrade bacterial cell walls, but proteins involved in many other biological functions also contain this domain. It has been reported that the LysM domain functions as a signal for specific plant-bacteria recognition in bacterial pathogenesis. Many of these enzymes are modular and are composed of catalytic units linked to one or several repeats of LysM domains. LysM domains are found in bacteria and eukaryotes.
pfam01476 LysM 1.76e-15 403 446 1 43
LysM domain. The LysM (lysin motif) domain is about 40 residues long. It is found in a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. The structure of this domain is known.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCK83709.1 3.07e-301 1 447 1 447
QHZ47012.1 2.77e-10 399 445 214 260
CDM70433.1 6.98e-10 374 446 194 266
ASB88452.1 8.99e-10 385 445 203 261
QFG73306.1 1.27e-09 388 445 408 464

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3TM1_A 4.69e-54 38 369 57 405
Crystalstructure of mature ThnT, a pantetheine hydrolase [Streptomyces cattleya],3TM1_B Crystal structure of mature ThnT, a pantetheine hydrolase [Streptomyces cattleya],3TM2_A Crystal structure of mature ThnT with a covalently bound product mimic [Streptomyces cattleya],3TM2_B Crystal structure of mature ThnT with a covalently bound product mimic [Streptomyces cattleya]
4IHE_A 2.50e-53 38 369 57 405
CrystalStructure of Uncleaved ThnT T282A [Streptomyces cattleya],4IHE_B Crystal Structure of Uncleaved ThnT T282A [Streptomyces cattleya]
3S3U_A 3.50e-53 38 369 57 405
CrystalStructure of Uncleaved ThnT T282C [Streptomyces cattleya],3S3U_B Crystal Structure of Uncleaved ThnT T282C [Streptomyces cattleya],4IHD_A Crystal Structure of Uncleaved ThnT T282C, derivatized at the active site with EtHg [Streptomyces cattleya],4IHD_B Crystal Structure of Uncleaved ThnT T282C, derivatized at the active site with EtHg [Streptomyces cattleya]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P64812 5.01e-50 38 358 6 332
Uncharacterized aminopeptidase Mb1368 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) OX=233413 GN=BQ2027_MB1368 PE=3 SV=1
P9WM22 5.01e-50 38 358 6 332
Uncharacterized aminopeptidase MT1375 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT1375 PE=3 SV=1
P9WM23 5.01e-50 38 358 6 332
Uncharacterized aminopeptidase Rv1333 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv1333 PE=1 SV=1
P53425 2.15e-49 38 362 13 347
Uncharacterized aminopeptidase ML1167 OS=Mycobacterium leprae (strain TN) OX=272631 GN=ML1167 PE=3 SV=1
Q5HRU2 6.19e-07 396 444 79 126
N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 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
0.000202 0.999190 0.000165 0.000160 0.000145 0.000134

TMHMM  Annotations      download full data without filtering help

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