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CAZyme Information: MGYG000000343_02261

You are here: Home > Sequence: MGYG000000343_02261

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 Odoribacter sp900548135
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Marinifilaceae; Odoribacter; Odoribacter sp900548135
CAZyme ID MGYG000000343_02261
CAZy Family GH33
CAZyme Description Arylsulfatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
473 52435.35 6.8755
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000343 3841231 MAG Sweden Europe
Gene Location Start: 48193;  End: 49614  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000343_02261.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16026 GALNS_like 0.0 25 429 3 399
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 9.11e-124 25 441 2 416
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 8.49e-122 25 429 2 395
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.
cd16142 ARS_like 5.87e-120 25 428 2 371
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.
cd16146 ARS_like 4.87e-119 25 439 2 397
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VTR91273.1 4.55e-163 1 473 1 476
VTS00049.1 1.04e-156 1 470 1 477
AWM40795.1 1.04e-156 1 470 1 477
QEG25923.1 1.04e-156 1 470 1 477
QNN23223.1 2.64e-103 25 450 34 429

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1E1Z_P 3.38e-76 25 447 4 442
Crystalstructure of an Arylsulfatase A mutant C69S [Homo sapiens]
1E3C_P 3.38e-76 25 447 4 442
Crystalstructure of an Arylsulfatase A mutant C69S soaked in synthetic substrate [Homo sapiens]
1E2S_P 9.38e-76 25 447 4 442
Crystalstructure of an Arylsulfatase A mutant C69A [Homo sapiens]
1AUK_A 1.85e-75 25 447 4 442
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]
1E33_P 1.85e-75 25 447 4 442
Crystalstructure of an Arylsulfatase A mutant P426L [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P50428 2.09e-79 25 447 21 459
Arylsulfatase A OS=Mus musculus OX=10090 GN=Arsa PE=1 SV=2
Q571E4 1.26e-77 7 450 10 477
N-acetylgalactosamine-6-sulfatase OS=Mus musculus OX=10090 GN=Galns PE=1 SV=2
Q32KJ6 1.50e-76 6 450 13 481
N-acetylgalactosamine-6-sulfatase OS=Rattus norvegicus OX=10116 GN=Galns PE=1 SV=1
Q32KH5 5.54e-76 5 450 12 479
N-acetylgalactosamine-6-sulfatase OS=Canis lupus familiaris OX=9615 GN=GALNS PE=2 SV=1
P15289 1.60e-74 25 447 22 460
Arylsulfatase A OS=Homo sapiens OX=9606 GN=ARSA PE=1 SV=3

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
0.000217 0.999156 0.000161 0.000170 0.000149 0.000140

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000343_02261.