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CAZyme Information: MGYG000000054_00743

You are here: Home > Sequence: MGYG000000054_00743

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 Bacteroides acidifaciens
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides acidifaciens
CAZyme ID MGYG000000054_00743
CAZy Family CE7
CAZyme Description Acetyl esterase Axe7A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
433 49138.76 9.4308
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000054 5213730 Isolate United Kingdom Europe
Gene Location Start: 38179;  End: 39480  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000054_00743.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 128 421 3.1e-83 0.9584664536741214

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3458 Axe1 5.32e-40 136 428 21 316
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448 AXE1 2.32e-37 128 408 12 299
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBK67089.1 6.10e-312 1 431 1 432
QUT79463.1 1.23e-311 1 431 1 432
QDM10171.1 1.23e-311 1 431 1 432
QDH53354.1 1.75e-311 1 431 1 432
QRM99767.1 2.48e-311 1 431 1 432

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6AGQ_A 1.71e-28 130 408 15 303
Acetylxylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_B Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_C Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_D Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_E Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4],6AGQ_F Acetyl xylan esterase from Paenibacillus sp. R4 [Paenibacillus sp. R4]
5HFN_A 9.65e-28 127 408 24 289
Crystalstructure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_B Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_C Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_D Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_E Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8],5HFN_F Crystal structure of a loop truncation variant of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 2.75 Angstrom resolution [Thermotoga maritima MSB8]
1ODS_A 3.94e-27 130 408 15 298
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]
1L7A_A 3.94e-27 130 408 15 298
structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
5GMA_A 5.48e-27 127 408 24 315
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D5EXI2 3.35e-95 35 413 46 425
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
P94388 1.57e-26 130 408 15 298
Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2 4.61e-26 127 408 12 303
Cephalosporin-C deacetylase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=axeA PE=1 SV=1

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
0.000279 0.999048 0.000174 0.000169 0.000153 0.000140

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000054_00743.