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CAZyme Information: MGYG000004688_00555

You are here: Home > Sequence: MGYG000004688_00555

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 CAG-873 sp900550395
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900550395
CAZyme ID MGYG000004688_00555
CAZy Family CE7
CAZyme Description Acetyl esterase Axe7A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
431 48277.14 8.7359
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004688 2658373 MAG Spain Europe
Gene Location Start: 5501;  End: 6796  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004688_00555.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 124 418 7.5e-82 0.9584664536741214

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3458 Axe1 1.90e-43 115 426 1 321
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448 AXE1 3.12e-41 126 399 14 293
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.
COG1506 DAP2 1.63e-04 273 389 460 575
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
COG4287 PqaA 3.65e-04 268 405 215 369
PhoPQ-activated pathogenicity-related protein [General function prediction only].
COG0412 DLH 0.001 179 318 11 145
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBK67089.1 8.42e-191 4 423 9 427
QRM99767.1 3.41e-190 4 423 9 427
QDH53354.1 7.95e-189 4 423 9 427
QUT26113.1 7.95e-189 5 423 7 427
QUR45652.1 1.60e-188 5 423 7 427

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6AGQ_A 1.28e-29 123 405 12 303
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]
5GMA_A 5.78e-28 123 405 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]
5HFN_A 2.45e-27 123 405 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]
3M81_A 2.83e-27 123 405 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]
1VLQ_A 7.34e-27 123 405 24 315
Crystalstructure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_B Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_C Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_D Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_E Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_F Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_G Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_H Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_I Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_J Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_K Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [Thermotoga maritima MSB8],1VLQ_L Crystal structure of Acetyl xylan esterase (TM0077) from Thermotoga maritima at 2.10 A resolution [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 4.97e-94 8 419 22 434
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
Q9WXT2 1.26e-26 123 405 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
P94388 6.90e-25 123 399 12 292
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
0.000337 0.998876 0.000199 0.000205 0.000197 0.000184

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004688_00555.