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CAZyme Information: MGYG000001364_01095

You are here: Home > Sequence: MGYG000001364_01095

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 Phocaeicola plebeius
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola plebeius
CAZyme ID MGYG000001364_01095
CAZy Family GH16
CAZyme Description Arylsulfatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
515 MGYG000001364_3|CGC7 58332.96 6.3938
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001364 4421324 Isolate not provided Asia
Gene Location Start: 412497;  End: 414044  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001364_01095.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16144 ARS_like 2.99e-172 26 491 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.
cd16146 ARS_like 7.15e-91 26 491 1 404
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 2.98e-80 26 478 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 6.56e-73 25 474 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 2.04e-72 24 473 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
QUT89376.1 2.20e-170 1 513 1 498
ALJ59588.1 4.95e-169 1 513 1 498
EAR02039.1 7.66e-163 25 515 28 511
AKJ65363.1 1.73e-63 24 501 25 453
QDV24880.1 1.30e-37 17 486 464 896

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6USS_A 2.77e-184 25 515 33 517
ChainA, Sulfatase [Bacteroides fragilis CAG:558],6USS_B Chain B, Sulfatase [Bacteroides fragilis CAG:558]
6UST_A 8.60e-58 25 502 4 463
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 7.34e-54 21 507 2 448
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 8.08e-44 25 491 2 418
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 8.23e-44 25 491 2 418
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 8.19e-47 13 512 22 543
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
Q9C0V7 6.31e-36 25 484 11 519
Uncharacterized sulfatase PB10D8.02c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=SPBPB10D8.02c PE=3 SV=1
Q32KH5 2.99e-33 26 421 30 385
N-acetylgalactosamine-6-sulfatase OS=Canis lupus familiaris OX=9615 GN=GALNS PE=2 SV=1
P34059 1.40e-32 26 486 31 467
N-acetylgalactosamine-6-sulfatase OS=Homo sapiens OX=9606 GN=GALNS PE=1 SV=1
P51691 1.62e-32 25 492 4 521
Arylsulfatase OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=atsA 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
0.000489 0.997438 0.001409 0.000257 0.000208 0.000172

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001364_01095.