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CAZyme Information: MGYG000001391_00527

You are here: Home > Sequence: MGYG000001391_00527

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 Coprobacter fastidiosus
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter fastidiosus
CAZyme ID MGYG000001391_00527
CAZy Family GH16
CAZyme Description Arylsulfatase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
511 57912.64 5.3757
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001391 3843461 Isolate not provided not provided
Gene Location Start: 600070;  End: 601605  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001391_00527.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd16144 ARS_like 1.28e-169 29 485 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.
cd16145 ARS_like 5.77e-87 29 472 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.
cd16146 ARS_like 9.57e-84 29 470 1 388
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.
cd16026 GALNS_like 1.13e-81 28 469 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 8.22e-78 27 468 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 3.88e-195 25 510 20 498
ALJ59588.1 8.82e-194 25 510 20 498
EAR02039.1 2.01e-152 28 511 28 510
AKJ65363.1 6.88e-61 27 497 25 452
BAX82390.1 1.66e-42 9 499 12 450

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6USS_A 1.22e-166 28 511 33 516
ChainA, Sulfatase [Bacteroides fragilis CAG:558],6USS_B Chain B, Sulfatase [Bacteroides fragilis CAG:558]
7STT_A 1.38e-62 23 469 1 415
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]
6UST_A 7.11e-61 28 471 4 437
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]
6B0K_A 3.93e-44 27 470 1 402
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 4.01e-44 27 470 1 402
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 1.19e-50 2 490 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
P50429 2.37e-33 17 407 34 384
Arylsulfatase B OS=Mus musculus OX=10090 GN=Arsb PE=1 SV=3
Q571E4 9.56e-33 20 417 19 383
N-acetylgalactosamine-6-sulfatase OS=Mus musculus OX=10090 GN=Galns PE=1 SV=2
Q32KH5 1.81e-32 25 417 26 385
N-acetylgalactosamine-6-sulfatase OS=Canis lupus familiaris OX=9615 GN=GALNS PE=2 SV=1
Q32KJ6 2.52e-32 7 417 3 387
N-acetylgalactosamine-6-sulfatase OS=Rattus norvegicus OX=10116 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
0.001760 0.996910 0.000621 0.000252 0.000223 0.000205

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001391_00527.