Species | Prevotella sp900553965 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900553965 | |||||||||||
CAZyme ID | MGYG000001806_01090 | |||||||||||
CAZy Family | CE7 | |||||||||||
CAZyme Description | Acetyl esterase Axe7A | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 3108; End: 4412 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE7 | 128 | 422 | 9.4e-81 | 0.9616613418530351 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam05448 | AXE1 | 1.07e-45 | 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. |
COG3458 | Axe1 | 6.46e-45 | 128 | 427 | 13 | 319 | Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism]. |
COG1506 | DAP2 | 3.55e-10 | 144 | 409 | 339 | 595 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
COG0412 | DLH | 1.85e-04 | 276 | 324 | 98 | 146 | Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]. |
COG4287 | PqaA | 8.90e-04 | 284 | 419 | 228 | 380 | PhoPQ-activated pathogenicity-related protein [General function prediction only]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AKQ46436.1 | 1.03e-117 | 29 | 424 | 32 | 430 |
ALI97837.1 | 6.65e-116 | 19 | 424 | 22 | 430 |
BAV05336.1 | 4.71e-114 | 16 | 428 | 16 | 430 |
ALK84253.1 | 1.03e-112 | 24 | 424 | 25 | 433 |
QQY39133.1 | 1.46e-112 | 24 | 424 | 25 | 433 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6AGQ_A | 1.84e-29 | 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] |
1L7A_A | 6.26e-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 | 8.63e-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 | 2.25e-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] |
5GMA_A | 4.60e-25 | 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 | 2.42e-104 | 2 | 424 | 14 | 436 | Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1 |
P94388 | 4.72e-28 | 128 | 424 | 13 | 314 | Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1 |
Q9WXT2 | 2.07e-24 | 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 |
---|---|---|---|---|---|
0.000584 | 0.998592 | 0.000199 | 0.000226 | 0.000188 | 0.000179 |
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