| Species | Bacteroides sp902388495 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp902388495 | |||||||||||
| CAZyme ID | MGYG000002561_00698 | |||||||||||
| CAZy Family | CE7 | |||||||||||
| CAZyme Description | Acetyl esterase Axe7A | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 55228; End: 56577 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE7 | 140 | 443 | 6.5e-88 | 0.9616613418530351 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3458 | Axe1 | 1.04e-42 | 139 | 429 | 9 | 299 | Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism]. |
| pfam05448 | AXE1 | 2.91e-42 | 139 | 429 | 8 | 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. |
| COG1506 | DAP2 | 1.54e-10 | 195 | 449 | 375 | 619 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
| pfam00326 | Peptidase_S9 | 5.97e-06 | 235 | 416 | 9 | 171 | Prolyl oligopeptidase family. |
| pfam01738 | DLH | 0.004 | 200 | 342 | 2 | 128 | Dienelactone hydrolase family. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AVM56440.1 | 3.61e-284 | 18 | 447 | 6 | 435 |
| QDO69181.1 | 1.85e-282 | 21 | 447 | 10 | 437 |
| QUT93205.1 | 6.16e-281 | 20 | 447 | 9 | 437 |
| ALJ61266.1 | 6.16e-281 | 20 | 447 | 9 | 437 |
| AVM53955.1 | 2.32e-280 | 18 | 447 | 6 | 435 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6AGQ_A | 1.11e-28 | 142 | 420 | 15 | 294 | 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] |
| 1L7A_A | 2.90e-25 | 136 | 420 | 14 | 289 | structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis] |
| 1ODS_A | 7.44e-25 | 136 | 420 | 14 | 289 | 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] |
| 1ODT_C | 1.02e-24 | 136 | 420 | 14 | 289 | cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis] |
| 5GMA_A | 2.58e-24 | 139 | 429 | 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] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D5EXI2 | 1.75e-209 | 29 | 447 | 28 | 438 | Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1 |
| P94388 | 1.59e-24 | 136 | 420 | 14 | 289 | Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1 |
| Q9WXT2 | 1.17e-23 | 139 | 429 | 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 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.001412 | 0.997665 | 0.000223 | 0.000268 | 0.000201 | 0.000189 |
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