| Species | Phocaeicola sp900544675 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Phocaeicola; Phocaeicola sp900544675 | |||||||||||
| CAZyme ID | MGYG000001925_01898 | |||||||||||
| CAZy Family | CE7 | |||||||||||
| CAZyme Description | Acetyl esterase Axe7A | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 26263; End: 27570 Strand: + | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE7 | 131 | 430 | 8.9e-92 | 0.9648562300319489 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam05448 | AXE1 | 2.58e-50 | 131 | 416 | 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. |
| COG3458 | Axe1 | 5.46e-49 | 131 | 416 | 9 | 299 | Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism]. |
| COG1506 | DAP2 | 1.67e-11 | 187 | 435 | 375 | 618 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
| COG0412 | DLH | 2.14e-07 | 186 | 396 | 10 | 214 | Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]. |
| pfam01738 | DLH | 1.75e-04 | 192 | 328 | 2 | 128 | Dienelactone hydrolase family. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ADY37130.1 | 9.16e-285 | 4 | 435 | 2 | 433 |
| QQY39133.1 | 3.00e-240 | 20 | 435 | 17 | 436 |
| ABR39032.1 | 3.00e-240 | 20 | 435 | 17 | 436 |
| QQY42402.1 | 3.00e-240 | 20 | 435 | 17 | 436 |
| QUT56063.1 | 3.00e-240 | 20 | 435 | 17 | 436 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1ODS_A | 7.01e-31 | 131 | 435 | 9 | 317 | 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 | 1.85e-30 | 131 | 435 | 9 | 317 | cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis] |
| 1L7A_A | 4.85e-30 | 131 | 435 | 9 | 317 | structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis] |
| 6AGQ_A | 5.86e-27 | 132 | 434 | 10 | 321 | 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 | 9.65e-26 | 131 | 416 | 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 | 1.07e-204 | 24 | 435 | 31 | 439 | Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1 |
| P94388 | 3.84e-30 | 131 | 435 | 9 | 317 | Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1 |
| Q9WXT2 | 5.94e-25 | 131 | 416 | 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 |
|---|---|---|---|---|---|
| 0.000657 | 0.998533 | 0.000298 | 0.000175 | 0.000166 | 0.000166 |
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