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CAZyme Information: MGYG000001056_01843

You are here: Home > Sequence: MGYG000001056_01843

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_01843
CAZy Family CE7
CAZyme Description Acetyl esterase Axe7A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
434 48561.47 7.9764
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001056 3020119 MAG Spain Europe
Gene Location Start: 270;  End: 1574  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001056_01843.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 128 426 5.4e-79 0.952076677316294

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3458 Axe1 3.58e-42 127 418 13 303
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448 AXE1 3.16e-38 134 414 19 299
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.
pfam10142 PhoPQ_related 1.21e-05 270 415 150 302
PhoPQ-activated pathogenicity-related protein. Members of this family of bacterial proteins are involved in the virulence of some pathogenic proteobacteria.
COG0412 DLH 1.25e-05 260 373 83 195
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism].
COG4287 PqaA 1.38e-05 269 415 213 370
PhoPQ-activated pathogenicity-related protein [General function prediction only].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QNT67783.1 4.44e-254 15 434 3 429
BCS86240.1 2.16e-221 34 433 2 396
AGH13969.1 2.48e-213 15 428 5 410
ADD61405.1 9.88e-175 1 433 1 424
QMI79435.1 9.88e-175 1 433 1 424

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1L7A_A 3.10e-28 123 414 14 298
structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
1ODS_A 8.10e-28 123 414 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]
5GMA_A 1.14e-27 126 414 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]
3M81_A 1.56e-27 126 414 24 315
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]
1ODT_C 2.11e-27 123 414 14 298
cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [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 1.62e-72 26 415 37 421
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
P94388 3.22e-27 123 414 14 298
Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2 6.93e-27 126 414 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
0.000484 0.998457 0.000452 0.000208 0.000196 0.000182

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001056_01843.