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CAZyme Information: MGYG000003295_00874

You are here: Home > Sequence: MGYG000003295_00874

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 sp002437405
Lineage Bacteria; Verrucomicrobiota; Verrucomicrobiae; Opitutales; CAG-312; CAG-312; CAG-312 sp002437405
CAZyme ID MGYG000003295_00874
CAZy Family CE7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
662 72659.13 8.6091
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003295 2127186 MAG Mongolia Asia
Gene Location Start: 1899;  End: 3887  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003295_00874.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 367 648 1.8e-49 0.9265175718849841

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam05448 AXE1 1.00e-25 373 648 18 303
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 4.77e-23 374 637 20 292
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506 DAP2 6.50e-06 386 620 354 567
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 1.31e-244 20 653 15 652
AVM47267.1 1.18e-147 203 652 68 508
SDU24469.1 6.42e-110 256 652 20 410
AVM46416.1 3.90e-104 256 657 23 413
AVM45740.1 3.79e-98 203 648 107 556

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6AGQ_A 7.54e-19 369 648 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 1.41e-17 375 648 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 1.90e-17 375 648 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 3.45e-17 375 648 21 302
cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis]
3FVR_A 5.66e-14 377 648 23 302
CrystalStructure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_B Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_C Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_D Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_E Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_F Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_G Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_H Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_I Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_L Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_M Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVR_N Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form I [Bacillus pumilus],3FVT_A Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_B Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_C Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_D Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_E Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_F Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_G Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_H Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_I Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_L Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_M Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FVT_N Crystal Structure of Acetyl Xylan Esterase from Bacillus pumilus, monoclinic crystal form II [Bacillus pumilus],3FYU_C Crystal structure of acetyl xylan esterase from Bacillus pumilus obtained in presence of D-xylose and sodium acetate [Bacillus pumilus],3FYU_E Crystal structure of acetyl xylan esterase from Bacillus pumilus obtained in presence of D-xylose and sodium acetate [Bacillus pumilus],3FYU_F Crystal structure of acetyl xylan esterase from Bacillus pumilus obtained in presence of D-xylose and sodium acetate [Bacillus pumilus],3FYU_G Crystal structure of acetyl xylan esterase from Bacillus pumilus obtained in presence of D-xylose and sodium acetate [Bacillus pumilus],3FYU_L Crystal structure of acetyl xylan esterase from Bacillus pumilus obtained in presence of D-xylose and sodium acetate [Bacillus pumilus],3FYU_M Crystal structure of acetyl xylan esterase from Bacillus pumilus obtained in presence of D-xylose and sodium acetate [Bacillus pumilus],3FYU_N Crystal structure of acetyl xylan esterase from Bacillus pumilus obtained in presence of D-xylose and sodium acetate [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 1.16e-24 368 634 136 410
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
P94388 7.74e-17 375 648 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 SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000650 0.998482 0.000269 0.000224 0.000186 0.000157

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003295_00874.