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CAZyme Information: MGYG000000013_03164

You are here: Home > Sequence: MGYG000000013_03164

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 sp902362375
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp902362375
CAZyme ID MGYG000000013_03164
CAZy Family GH33
CAZyme Description Arylsulfatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
466 MGYG000000013_7|CGC8 51350 5.3095
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000013 6368149 Isolate United Kingdom Europe
Gene Location Start: 385460;  End: 386860  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000013_03164.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16026 GALNS_like 0.0 39 439 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 1.36e-122 40 457 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.
cd16143 ARS_like 1.23e-118 40 440 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.
cd16146 ARS_like 3.16e-118 40 450 1 397
uncharacterized arylsulfatase. 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.
cd16145 ARS_like 1.73e-116 40 444 1 415
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
VTR91273.1 6.35e-130 36 450 20 442
VTS00049.1 2.53e-124 36 465 20 461
AWM40795.1 2.53e-124 36 465 20 461
QEG25923.1 2.53e-124 36 465 20 461
QDT08292.1 5.69e-107 39 462 735 1155

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1E33_P 1.40e-76 40 450 3 438
Crystalstructure of an Arylsulfatase A mutant P426L [Homo sapiens]
1E1Z_P 2.77e-76 40 450 3 438
Crystalstructure of an Arylsulfatase A mutant C69S [Homo sapiens]
1E3C_P 2.77e-76 40 450 3 438
Crystalstructure of an Arylsulfatase A mutant C69S soaked in synthetic substrate [Homo sapiens]
1E2S_P 7.69e-76 40 450 3 438
Crystalstructure of an Arylsulfatase A mutant C69A [Homo sapiens]
1AUK_A 1.52e-75 40 450 3 438
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
Q08DD1 7.47e-82 36 463 17 465
Arylsulfatase A OS=Bos taurus OX=9913 GN=ARSA PE=2 SV=1
P15289 4.73e-75 37 450 18 456
Arylsulfatase A OS=Homo sapiens OX=9606 GN=ARSA PE=1 SV=3
P50428 1.79e-74 37 463 17 464
Arylsulfatase A OS=Mus musculus OX=10090 GN=Arsa PE=1 SV=2
Q96EG1 4.31e-73 38 456 34 492
Arylsulfatase G OS=Homo sapiens OX=9606 GN=ARSG PE=1 SV=1
Q3TYD4 1.27e-71 37 456 33 488
Arylsulfatase G OS=Mus musculus OX=10090 GN=Arsg PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000002 0.001173 0.998863 0.000000 0.000001 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000013_03164.