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CAZyme Information: MGYG000002455_03754

You are here: Home > Sequence: MGYG000002455_03754

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 Bacteroides cellulosilyticus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides cellulosilyticus
CAZyme ID MGYG000002455_03754
CAZy Family GH117
CAZyme Description Arylsulfatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
483 MGYG000002455_17|CGC1 54006.04 5.0587
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002455 6974062 Isolate United States North America
Gene Location Start: 81961;  End: 83412  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002455_03754.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16026 GALNS_like 0.0 33 413 1 398
galactosamine-6-sulfatase; also known as N-acetylgalactosamine-6-sulfatase (GALNS). Lysosomal galactosamine-6-sulfatase removes sulfate groups from a terminal N-acetylgalactosamine-6-sulfate (or galactose-6-sulfate) in mucopolysaccharides such as keratan sulfate and chondroitin-6-sulfate. Defects in GALNS lead to accumulation of substrates, resulting in the development of the lysosomal storage disease mucopolysaccharidosis IV A.
cd16144 ARS_like 4.40e-133 34 431 1 421
uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
cd16142 ARS_like 5.88e-131 34 413 1 371
uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.
cd16158 ARSA 2.13e-129 33 413 1 422
Arylsulfatase A or cerebroside-sulfatase. Arylsulfatase A breaks down sulfatides, namely cerebroside 3-sulfate into cerebroside and sulfate. It is a member of the sulfatase family. The arylsulfatase A was located in lysosome-like structures and transported to dense lysosomes in a mannose 6-phosphate receptor-dependent manner. Deficiency of arylsulfatase A leads to the accumulation of cerebroside sulfate, which causes a lethal progressive demyelination. Arylsulfatase A requires the posttranslational oxidation of the -CH2SH group of a conserved cysteine to an aldehyde, yielding a formylglycine to be in an active form.
cd16143 ARS_like 5.99e-123 34 414 1 395
uncharacterized arylsulfatase subfamily. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDH57428.1 2.34e-113 32 431 21 456
QNN23223.1 1.28e-108 10 441 13 437
VTR91273.1 1.63e-100 31 437 21 455
QDT95903.1 7.53e-96 19 438 23 466
QDU36023.1 7.02e-95 24 437 30 478

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1E1Z_P 4.31e-92 32 430 1 440
Crystalstructure of an Arylsulfatase A mutant C69S [Homo sapiens]
1E3C_P 4.31e-92 32 430 1 440
Crystalstructure of an Arylsulfatase A mutant C69S soaked in synthetic substrate [Homo sapiens]
1E2S_P 1.21e-91 32 430 1 440
Crystalstructure of an Arylsulfatase A mutant C69A [Homo sapiens]
1E33_P 2.39e-91 32 430 1 440
Crystalstructure of an Arylsulfatase A mutant P426L [Homo sapiens]
1AUK_A 2.39e-91 32 430 1 440
HumanArylsulfatase A [Homo sapiens],1N2K_A Crystal structure of a covalent intermediate of endogenous human arylsulfatase A [Homo sapiens],1N2L_A Crystal structure of a covalent intermediate of endogenous human arylsulfatase A [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P15289 1.53e-90 31 430 18 458
Arylsulfatase A OS=Homo sapiens OX=9606 GN=ARSA PE=1 SV=3
P50428 1.19e-85 16 429 3 456
Arylsulfatase A OS=Mus musculus OX=10090 GN=Arsa PE=1 SV=2
Q08DD1 3.42e-85 31 430 18 458
Arylsulfatase A OS=Bos taurus OX=9913 GN=ARSA PE=2 SV=1
Q32KH5 3.47e-77 32 432 28 469
N-acetylgalactosamine-6-sulfatase OS=Canis lupus familiaris OX=9615 GN=GALNS PE=2 SV=1
Q8WNQ7 1.35e-76 15 413 15 454
N-acetylgalactosamine-6-sulfatase OS=Sus scrofa OX=9823 GN=GALNS PE=2 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
0.002026 0.752848 0.244040 0.000528 0.000276 0.000242

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002455_03754.