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CAZyme Information: MGYG000003201_01064

You are here: Home > Sequence: MGYG000003201_01064

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-873 sp900759825
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; CAG-873; CAG-873 sp900759825
CAZyme ID MGYG000003201_01064
CAZy Family CE7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
965 105523.58 4.4793
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003201 2637500 MAG United States North America
Gene Location Start: 55;  End: 2952  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003201_01064.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 573 880 9.4e-54 0.9169329073482428
CE7 19 219 4.8e-35 0.6070287539936102

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam05448 AXE1 9.46e-35 576 882 21 308
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 1.45e-31 576 853 22 283
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448 AXE1 3.01e-22 44 206 142 299
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 3.96e-15 45 190 145 289
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506 DAP2 0.001 595 803 346 543
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB71398.1 7.40e-145 237 917 27 691
SJX74200.1 3.86e-66 536 891 198 528
BCI63353.1 1.07e-59 540 855 115 407
CBK67642.1 4.28e-59 539 892 101 426
QRM99272.1 4.74e-59 539 892 105 430

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6AGQ_A 6.68e-23 577 853 23 287
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]
3FCY_A 4.39e-18 576 874 48 328
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]
3FVR_A 8.56e-16 27 222 124 314
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]
2XLB_A 1.15e-15 27 222 124 314
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]
2XLC_A 1.15e-15 27 222 124 314
Acetylxylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_B Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_C Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_D Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_E Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus],2XLC_F Acetyl xylan esterase from Bacillus pumilus CECT5072 bound to paraoxon [Bacillus pumilus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9WXT2 9.45e-14 576 853 22 287
Cephalosporin-C deacetylase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=axeA PE=1 SV=1
D5EXI2 1.34e-13 40 211 265 425
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
P94388 1.22e-12 44 222 141 314
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 OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000002 0.000037 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003201_01064.