logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000003856_00975

You are here: Home > Sequence: MGYG000003856_00975

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 Paramuribaculum sp900551515
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; Paramuribaculum; Paramuribaculum sp900551515
CAZyme ID MGYG000003856_00975
CAZy Family GH16
CAZyme Description Arylsulfatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
535 MGYG000003856_34|CGC1 58588.82 5.0897
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003856 2220083 MAG United States North America
Gene Location Start: 2056;  End: 3663  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003856_00975.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16144 ARS_like 1.78e-175 28 490 1 418
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 1.00e-91 28 492 1 403
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 6.92e-86 28 480 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.
cd16026 GALNS_like 2.83e-82 27 476 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.
cd16025 PAS_like 3.57e-82 26 475 1 402
Bacterial Arylsulfatase of Pseudomonas aeruginosa and related 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
EAR02039.1 2.96e-153 27 516 28 511
QUT89376.1 6.98e-151 14 514 9 498
ALJ59588.1 2.19e-149 14 514 9 498
AKJ65363.1 4.60e-64 27 502 26 452
QGJ68845.1 1.84e-48 28 486 27 441

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6USS_A 6.07e-181 3 516 1 517
ChainA, Sulfatase [Bacteroides fragilis CAG:558],6USS_B Chain B, Sulfatase [Bacteroides fragilis CAG:558]
6UST_A 4.31e-75 25 502 2 461
ChainA, N-acetylgalactosamine 6-sulfate sulfatase [Hungatella hathewayi],6UST_B Chain B, N-acetylgalactosamine 6-sulfate sulfatase [Hungatella hathewayi],6UST_C Chain C, N-acetylgalactosamine 6-sulfate sulfatase [Hungatella hathewayi],6UST_D Chain D, N-acetylgalactosamine 6-sulfate sulfatase [Hungatella hathewayi]
7STT_A 1.33e-60 27 502 6 441
ChainA, N-acetylgalactosamine-6-sulfatase [Pedobacter yulinensis],7STU_A Chain A, N-acetylgalactosamine-6-sulfatase [Pedobacter yulinensis],7STV_A Chain A, N-acetylgalactosamine-6-sulfatase [Pedobacter yulinensis]
6B0K_A 1.28e-47 27 488 2 413
Crystalstructure of Ps i-CgsB C78S in complex with k-carrapentaose [Pseudoalteromonas],6B0K_B Crystal structure of Ps i-CgsB C78S in complex with k-carrapentaose [Pseudoalteromonas],6B0K_C Crystal structure of Ps i-CgsB C78S in complex with k-carrapentaose [Pseudoalteromonas]
6B0J_A 1.30e-47 27 488 2 413
Crystalstructure of Ps i-CgsB in complex with k-i-k-neocarrahexaose [Pseudoalteromonas],6B0J_B Crystal structure of Ps i-CgsB in complex with k-i-k-neocarrahexaose [Pseudoalteromonas],6B0J_C Crystal structure of Ps i-CgsB in complex with k-i-k-neocarrahexaose [Pseudoalteromonas],6B1V_A Crystal structure of Ps i-CgsB C78S in complex with i-neocarratetraose [Pseudoalteromonas],6B1V_B Crystal structure of Ps i-CgsB C78S in complex with i-neocarratetraose [Pseudoalteromonas],6B1V_C Crystal structure of Ps i-CgsB C78S in complex with i-neocarratetraose [Pseudoalteromonas]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
T2KPJ9 1.07e-44 2 495 7 520
Sulfatase OS=Formosa agariphila (strain DSM 15362 / KCTC 12365 / LMG 23005 / KMM 3901 / M-2Alg 35-1) OX=1347342 GN=BN863_22020 PE=3 SV=1
Q32KH5 1.95e-41 28 455 30 403
N-acetylgalactosamine-6-sulfatase OS=Canis lupus familiaris OX=9615 GN=GALNS PE=2 SV=1
Q32KJ6 1.24e-39 5 461 11 413
N-acetylgalactosamine-6-sulfatase OS=Rattus norvegicus OX=10116 GN=Galns PE=1 SV=1
Q571E4 2.20e-39 28 461 28 409
N-acetylgalactosamine-6-sulfatase OS=Mus musculus OX=10090 GN=Galns PE=1 SV=2
P34059 1.10e-38 28 529 31 514
N-acetylgalactosamine-6-sulfatase OS=Homo sapiens OX=9606 GN=GALNS PE=1 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
0.000666 0.998318 0.000301 0.000297 0.000221 0.000194

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003856_00975.