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CAZyme Information: MGYG000002832_01390

You are here: Home > Sequence: MGYG000002832_01390

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 sp900548195
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900548195
CAZyme ID MGYG000002832_01390
CAZy Family CE7
CAZyme Description Acetyl esterase Axe7A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
438 49541.69 7.8764
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002832 2701309 MAG United Republic of Tanzania Africa
Gene Location Start: 8512;  End: 9828  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002832_01390.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 124 422 3.5e-76 0.9488817891373802

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3458 Axe1 2.78e-36 125 422 13 313
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448 AXE1 4.95e-30 125 412 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
QNT67783.1 3.17e-160 16 430 6 427
QMI79435.1 1.95e-158 6 432 7 425
QBJ17988.1 1.95e-158 6 432 7 425
AGH13969.1 2.78e-158 19 433 8 417
SIP56249.1 5.56e-158 6 432 7 425

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GMA_A 1.14e-21 124 412 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 2.10e-21 124 412 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]
1L7A_A 2.19e-21 124 412 12 298
structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
1ODS_A 2.99e-21 124 412 12 298
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]
1VLQ_A 3.89e-21 124 412 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 1.06e-66 34 402 46 410
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
Q9WXT2 9.76e-21 124 412 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 1.20e-20 124 412 12 298
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
0.000287 0.996110 0.002936 0.000235 0.000208 0.000181

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002832_01390.