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CAZyme Information: MGYG000001056_00657

You are here: Home > Sequence: MGYG000001056_00657

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 Prevotella sp900556395
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900556395
CAZyme ID MGYG000001056_00657
CAZy Family CE2
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
571 64798.71 8.213
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001056 3020119 MAG Spain Europe
Gene Location Start: 24548;  End: 26263  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001056_00657.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE2 148 350 1.6e-50 0.9856459330143541
CE3 423 564 4.9e-16 0.6907216494845361

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd04501 SGNH_hydrolase_like_4 7.14e-58 394 567 2 180
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.
cd01831 Endoglucanase_E_like 1.15e-33 148 351 2 168
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
cd01828 sialate_O-acetylesterase_like2 3.43e-32 394 571 1 169
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.
pfam13472 Lipase_GDSL_2 4.09e-29 397 561 1 176
GDSL-like Lipase/Acylhydrolase family. This family of presumed lipases and related enzymes are similar to pfam00657.
cd01841 NnaC_like 2.11e-21 396 566 4 170
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCS85000.1 3.29e-147 3 359 1 359
QUB47786.1 3.03e-127 27 360 61 395
AGY53007.1 1.02e-90 26 357 27 356
QUT38028.1 2.38e-89 24 357 26 358
BBL06085.1 2.87e-89 24 359 35 366

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4IYJ_A 2.44e-60 371 566 7 204
Crystalstructure of a putative acylhydrolase (BACUNI_03406) from Bacteroides uniformis ATCC 8492 at 1.37 A resolution [Bacteroides uniformis ATCC 8492],4IYJ_B Crystal structure of a putative acylhydrolase (BACUNI_03406) from Bacteroides uniformis ATCC 8492 at 1.37 A resolution [Bacteroides uniformis ATCC 8492]
4PPY_A 7.05e-58 370 566 3 201
Crystalstructure of a putative acylhydrolase (BF3764) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343],4PPY_B Crystal structure of a putative acylhydrolase (BF3764) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343],4PPY_C Crystal structure of a putative acylhydrolase (BF3764) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343]
4HF7_A 2.07e-55 372 566 5 201
Crystalstructure of a GDSL-like lipase (BT0569) from Bacteroides thetaiotaomicron VPI-5482 at 1.77 A resolution [Bacteroides thetaiotaomicron VPI-5482]
3P94_A 2.14e-50 372 567 5 196
Crystalstructure of a GDSL-like Lipase (BDI_0976) from Parabacteroides distasonis ATCC 8503 at 1.93 A resolution [Parabacteroides distasonis ATCC 8503],3P94_B Crystal structure of a GDSL-like Lipase (BDI_0976) from Parabacteroides distasonis ATCC 8503 at 1.93 A resolution [Parabacteroides distasonis ATCC 8503],3P94_C Crystal structure of a GDSL-like Lipase (BDI_0976) from Parabacteroides distasonis ATCC 8503 at 1.93 A resolution [Parabacteroides distasonis ATCC 8503],3P94_D Crystal structure of a GDSL-like Lipase (BDI_0976) from Parabacteroides distasonis ATCC 8503 at 1.93 A resolution [Parabacteroides distasonis ATCC 8503]
2W9X_A 2.60e-27 37 348 34 350
Theactive site of a carbohydrate esterase displays divergent catalytic and non-catalytic binding functions [Cellvibrio japonicus],2W9X_B The active site of a carbohydrate esterase displays divergent catalytic and non-catalytic binding functions [Cellvibrio japonicus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
B3PDE5 1.29e-26 37 348 34 350
Acetylxylan esterase / glucomannan deacetylase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=ce2C PE=1 SV=1
B3PIB0 4.07e-24 26 357 32 358
Acetylxylan esterase / glucomannan deacetylase OS=Cellvibrio japonicus (strain Ueda107) OX=498211 GN=axe2C PE=1 SV=1
P10477 4.79e-23 51 357 510 814
Cellulase/esterase CelE OS=Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) OX=203119 GN=celE PE=1 SV=2

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
0.000494 0.998496 0.000280 0.000252 0.000243 0.000216

TMHMM  Annotations      download full data without filtering help

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