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CAZyme Information: MGYG000004495_01768

You are here: Home > Sequence: MGYG000004495_01768

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
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella;
CAZyme ID MGYG000004495_01768
CAZy Family CE7
CAZyme Description Acetyl esterase Axe7A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
434 MGYG000004495_29|CGC2 48807.52 7.7038
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004495 2923471 MAG Israel Asia
Gene Location Start: 39848;  End: 41152  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004495_01768.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 133 427 1.2e-76 0.9584664536741214

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3458 Axe1 1.45e-39 132 417 13 303
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448 AXE1 2.46e-33 128 413 13 299
Acetyl xylan esterase (AXE1). This family consists of several bacterial acetyl xylan esterase proteins. Acetyl xylan esterases are enzymes that hydrolyze the ester linkages of the acetyl groups in position 2 and/or 3 of the xylose moieties of natural acetylated xylan from hardwood. These enzymes are one of the accessory enzymes which are part of the xylanolytic system, together with xylanases, beta-xylosidases, alpha-arabinofuranosidases and methylglucuronidases; these are all required for the complete hydrolysis of xylan.
COG4287 PqaA 3.30e-04 275 414 214 370
PhoPQ-activated pathogenicity-related protein [General function prediction only].
COG0412 DLH 0.001 272 389 90 174
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism].
pfam10142 PhoPQ_related 0.002 275 414 150 302
PhoPQ-activated pathogenicity-related protein. Members of this family of bacterial proteins are involved in the virulence of some pathogenic proteobacteria.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNT67783.1 4.74e-228 25 431 8 427
BCS86240.1 1.02e-226 39 434 2 398
AGH13969.1 2.61e-215 22 431 3 414
QMI79435.1 7.23e-182 28 433 19 425
QBJ17988.1 7.23e-182 28 433 19 425

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GMA_A 9.54e-26 128 413 26 315
Crystalstructure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_B Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_C Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_D Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_E Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_F Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8]
3M81_A 1.79e-25 128 413 26 315
Crystalstructure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_B Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_C Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_D Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_E Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_F Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],5FDF_A Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_B Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_C Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_D Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_E Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_F Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5JIB_A Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_B Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_C Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_D Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_E Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_F Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8]
2XLB_A 2.54e-25 131 413 12 298
Acetylxylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_B Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_C Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_D Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_E Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_F Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_G Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_H Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_I Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_J Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_K Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_L Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus]
2XLC_A 4.78e-25 131 413 12 298
Acetylxylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_B Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_C Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_D Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_E Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_F Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus]
1ODS_A 6.33e-25 128 413 14 298
CephalosporinC deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_B Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_C Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_D Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_E Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_F Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_G Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis],1ODS_H Cephalosporin C deacetylase from Bacillus subtilis [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D5EXI2 2.48e-71 31 414 37 421
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
Q9WXT2 8.06e-25 128 413 14 303
Cephalosporin-C deacetylase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=axeA PE=1 SV=1
P94388 2.53e-24 128 413 14 298
Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah 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
0.000321 0.999013 0.000200 0.000147 0.000139 0.000128

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004495_01768.