dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000224_01291

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Basic Information help

Species

Bacteroides sp003545565

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp003545565

CAZyme ID

MGYG000000224_01291

CAZy Family

GH33

CAZyme Description

Arylsulfatase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
469	MGYG000000224_4\|CGC2	51924.77	6.0968

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000224	3747034	Isolate	China	Asia

Gene Location

Start: 95609; End: 97018 Strand: +

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000000224_01291.

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd16026	GALNS_like	0.0	37	438	1	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.
cd16146	ARS_like	2.67e-130	38	459	1	408	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.
cd16144	ARS_like	8.53e-126	38	455	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	1.58e-120	38	438	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.
cd16160	spARS_like	7.98e-116	37	391	1	368	sea urchin arylsulfatase-like. This family includes sea urchin arylsulfatase and its homologous proteins. 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	2.26e-135	33	448	19	442
VTS00049.1	5.47e-128	33	448	19	446
AWM40795.1	5.47e-128	33	448	19	446
QEG25923.1	5.47e-128	33	448	19	446
QDT08292.1	2.33e-107	20	459	724	1154

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1E1Z_P	1.78e-74	38	391	3	377	Crystalstructure of an Arylsulfatase A mutant C69S [Homo sapiens]
1E3C_P	1.78e-74	38	391	3	377	Crystalstructure of an Arylsulfatase A mutant C69S soaked in synthetic substrate [Homo sapiens]
1E33_P	3.52e-74	38	444	3	434	Crystalstructure of an Arylsulfatase A mutant P426L [Homo sapiens]
1E2S_P	4.94e-74	38	391	3	377	Crystalstructure of an Arylsulfatase A mutant C69A [Homo sapiens]
1AUK_A	9.74e-74	38	391	3	377	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	5.74e-78	38	456	21	460	Arylsulfatase A OS=Bos taurus OX=9913 GN=ARSA PE=2 SV=1
Q32KJ9	7.67e-76	37	446	35	477	Arylsulfatase G OS=Rattus norvegicus OX=10116 GN=Arsg PE=2 SV=1
Q3TYD4	1.13e-74	37	446	35	477	Arylsulfatase G OS=Mus musculus OX=10090 GN=Arsg PE=1 SV=1
P50428	7.59e-74	38	391	20	394	Arylsulfatase A OS=Mus musculus OX=10090 GN=Arsa PE=1 SV=2
P15289	8.35e-73	38	391	21	395	Arylsulfatase A OS=Homo sapiens OX=9606 GN=ARSA PE=1 SV=3

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
0.000001	0.000416	0.999629	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000224_01291.