Species | ||||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; Firm-11; | |||||||||||
CAZyme ID | MGYG000004168_00704 | |||||||||||
CAZy Family | CE7 | |||||||||||
CAZyme Description | Cephalosporin-C deacetylase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 41621; End: 42580 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
CE7 | 4 | 315 | 4.4e-105 | 0.987220447284345 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam05448 | AXE1 | 1.88e-133 | 4 | 318 | 3 | 315 | 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 | 3.54e-119 | 1 | 318 | 1 | 315 | Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism]. |
COG1506 | DAP2 | 3.33e-15 | 21 | 306 | 335 | 598 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
pfam00561 | Abhydrolase_1 | 5.53e-08 | 84 | 305 | 1 | 241 | alpha/beta hydrolase fold. This catalytic domain is found in a very wide range of enzymes. |
pfam12146 | Hydrolase_4 | 8.23e-08 | 85 | 305 | 6 | 233 | Serine aminopeptidase, S33. This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AIQ51745.1 | 4.35e-144 | 1 | 317 | 1 | 317 |
AIQ46134.1 | 1.24e-143 | 1 | 317 | 1 | 317 |
QYR20547.1 | 9.94e-141 | 1 | 317 | 1 | 317 |
QKS47765.1 | 1.36e-140 | 1 | 318 | 1 | 318 |
AZN40069.1 | 5.52e-140 | 1 | 318 | 1 | 318 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3FCY_A | 1.75e-134 | 1 | 318 | 27 | 343 | CrystalStructure of Acetyl Xylan Esterase 1 from Thermoanaerobacterium sp. JW/SL YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3FCY_B Crystal Structure of Acetyl Xylan Esterase 1 from Thermoanaerobacterium sp. JW/SL YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485],3FCY_C Crystal Structure of Acetyl Xylan Esterase 1 from Thermoanaerobacterium sp. JW/SL YS485 [Thermoanaerobacterium saccharolyticum JW/SL-YS485] |
7CUZ_A | 3.85e-85 | 14 | 310 | 10 | 306 | ChainA, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_B Chain B, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_C Chain C, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_D Chain D, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147] |
6AGQ_A | 1.24e-59 | 1 | 313 | 1 | 313 | 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] |
1ODS_A | 2.18e-56 | 1 | 318 | 1 | 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 | 6.10e-56 | 1 | 318 | 1 | 314 | cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P94388 | 2.37e-55 | 1 | 318 | 1 | 314 | Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1 |
Q9WXT2 | 1.07e-47 | 1 | 303 | 1 | 304 | 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 |
---|---|---|---|---|---|
1.000070 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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