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CAZyme Information: MGYG000003958_00288
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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 | CAG-312 sp900545715 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; CAG-312; CAG-312; CAG-312 sp900545715 | |||||||||||
| CAZyme ID | MGYG000003958_00288 | |||||||||||
| CAZy Family | CE7 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 342792; End: 344729 Strand: - | |||||||||||
CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| CE7 | 349 | 635 | 2.5e-49 | 0.9488817891373802 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam05448 | AXE1 | 6.21e-30 | 349 | 631 | 9 | 303 | 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 | 2.23e-27 | 349 | 631 | 10 | 303 | Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism]. |
| COG1506 | DAP2 | 0.003 | 408 | 603 | 378 | 567 | Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AVM45055.1 | 1.50e-251 | 21 | 635 | 33 | 651 |
| AVM47267.1 | 4.76e-151 | 237 | 642 | 108 | 514 |
| SDU24469.1 | 1.66e-115 | 253 | 639 | 34 | 414 |
| AVM46416.1 | 1.05e-109 | 239 | 638 | 21 | 411 |
| AHF91279.1 | 2.56e-102 | 253 | 642 | 38 | 432 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6AGQ_A | 4.94e-20 | 350 | 631 | 8 | 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 | 5.15e-19 | 360 | 631 | 21 | 302 | structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis] |
| 1ODS_A | 6.94e-19 | 360 | 631 | 21 | 302 | 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 | 1.26e-18 | 360 | 631 | 21 | 302 | cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis] |
| 2XLB_A | 1.59e-15 | 349 | 631 | 10 | 302 | Acetylxylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_B Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_C Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_D Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_E Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_F Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_G Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_H Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_I Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_J Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_K Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus],2XLB_L Acetyl xylan esterase from Bacillus pumilus without ligands [Bacillus pumilus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D5EXI2 | 3.89e-27 | 290 | 618 | 88 | 411 | Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1 |
| P94388 | 2.82e-18 | 360 | 631 | 21 | 302 | Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as LIPO
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 0.000357 | 0.400344 | 0.598819 | 0.000168 | 0.000154 | 0.000140 |