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CAZyme Information: MGYG000003338_01316
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Dysgonomonadaceae; Dysgonomonas; | |||||||||||
| CAZyme ID | MGYG000003338_01316 | |||||||||||
| CAZy Family | CE7 | |||||||||||
| CAZyme Description | Acetyl esterase Axe7A | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 215; End: 1501 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE7 | 126 | 422 | 1.5e-87 | 0.9648562300319489 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam05448 | AXE1 | 8.37e-50 | 113 | 424 | 11 | 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 | 2.60e-49 | 118 | 428 | 1 | 320 | Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism]. |
| COG0412 | DLH | 1.63e-07 | 192 | 428 | 21 | 232 | Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]. |
| COG1506 | DAP2 | 1.33e-06 | 183 | 428 | 376 | 615 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
| COG0596 | MhpC | 0.003 | 331 | 426 | 183 | 279 | Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QUU00463.1 | 2.32e-208 | 1 | 426 | 1 | 426 |
| QQA31833.1 | 2.32e-208 | 1 | 426 | 1 | 426 |
| QUT62253.1 | 2.32e-208 | 1 | 426 | 1 | 426 |
| QBJ20319.1 | 3.81e-207 | 1 | 426 | 1 | 426 |
| QMI79281.1 | 3.81e-207 | 1 | 426 | 1 | 426 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6AGQ_A | 1.37e-40 | 125 | 412 | 2 | 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] |
| 1ODS_A | 6.82e-34 | 126 | 417 | 12 | 307 | 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] |
| 1L7A_A | 9.45e-34 | 126 | 417 | 12 | 307 | structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis] |
| 1ODT_C | 1.82e-33 | 126 | 417 | 12 | 307 | cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis] |
| 5GMA_A | 4.97e-32 | 126 | 428 | 24 | 336 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D5EXI2 | 4.51e-100 | 34 | 423 | 46 | 435 | Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1 |
| P94388 | 3.73e-33 | 126 | 417 | 12 | 307 | Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1 |
| Q9WXT2 | 5.68e-31 | 126 | 428 | 12 | 324 | Cephalosporin-C deacetylase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=axeA PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as SP
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000299 | 0.998935 | 0.000212 | 0.000179 | 0.000182 | 0.000163 |