| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; | |||||||||||
| CAZyme ID | MGYG000002063_00035 | |||||||||||
| CAZy Family | CE7 | |||||||||||
| CAZyme Description | Acetyl esterase Axe7A | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 40745; End: 42049 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE7 | 128 | 422 | 9.8e-81 | 0.9616613418530351 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG3458 | Axe1 | 1.09e-44 | 128 | 427 | 13 | 319 | Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism]. |
| pfam05448 | AXE1 | 3.03e-44 | 130 | 424 | 14 | 316 | 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 | 5.80e-10 | 180 | 409 | 372 | 595 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
| COG0412 | DLH | 7.71e-05 | 276 | 324 | 98 | 146 | Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]. |
| pfam01738 | DLH | 0.001 | 278 | 322 | 84 | 128 | Dienelactone hydrolase family. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BAV05336.1 | 6.45e-117 | 11 | 428 | 11 | 430 |
| AKQ46436.1 | 8.29e-117 | 6 | 424 | 5 | 430 |
| ALK84253.1 | 8.05e-115 | 2 | 424 | 4 | 433 |
| QQY39133.1 | 1.14e-114 | 2 | 424 | 4 | 433 |
| QJR75027.1 | 1.14e-114 | 17 | 424 | 18 | 433 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 1L7A_A | 3.29e-29 | 128 | 425 | 13 | 315 | structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis] |
| 1ODS_A | 4.54e-29 | 128 | 424 | 13 | 314 | 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 | 1.19e-28 | 128 | 424 | 13 | 314 | cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis] |
| 6AGQ_A | 1.26e-28 | 130 | 412 | 15 | 307 | 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 | 3.01e-24 | 130 | 408 | 27 | 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 | 4.76e-107 | 6 | 424 | 17 | 436 | Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1 |
| P94388 | 2.49e-28 | 128 | 424 | 13 | 314 | Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1 |
| Q9WXT2 | 1.37e-23 | 130 | 408 | 15 | 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 |
|---|---|---|---|---|---|
| 0.000305 | 0.999038 | 0.000156 | 0.000181 | 0.000160 | 0.000144 |
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