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CAZyme Information: MGYG000003572_01211

You are here: Home > Sequence: MGYG000003572_01211

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 Prevotella sp900770025
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella; Prevotella sp900770025
CAZyme ID MGYG000003572_01211
CAZy Family CE7
CAZyme Description Acetyl esterase Axe7A
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
431 48580.09 8.8411
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003572 2050564 MAG Fiji Oceania
Gene Location Start: 8792;  End: 10087  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003572_01211.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 134 426 9.4e-82 0.9552715654952076

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3458 Axe1 1.48e-49 124 427 2 315
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam05448 AXE1 1.43e-43 138 412 18 299
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.
COG1506 DAP2 8.34e-08 187 426 375 613
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
COG0412 DLH 2.48e-05 279 328 97 146
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism].
pfam01738 DLH 1.42e-04 282 383 84 153
Dienelactone hydrolase family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ALI97837.1 3.41e-115 21 429 22 431
BAV05336.1 2.12e-114 20 429 18 427
AKQ46436.1 1.55e-113 31 429 32 431
APA00297.1 1.81e-111 31 428 30 426
ADY37130.1 9.11e-104 7 427 8 429

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1ODS_A 1.40e-34 131 412 9 298
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 1.94e-34 131 412 9 298
structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
1ODT_C 3.73e-34 131 412 9 298
cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis]
3FVR_A 1.11e-27 129 412 7 298
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]
3FYT_A 2.89e-27 129 412 7 298
ChainA, Acetyl xylan esterase [Bacillus pumilus],3FYT_B Chain B, Acetyl xylan esterase [Bacillus pumilus],3FYT_C Chain C, Acetyl xylan esterase [Bacillus pumilus],3FYT_D Chain D, Acetyl xylan esterase [Bacillus pumilus],3FYT_E Chain E, Acetyl xylan esterase [Bacillus pumilus],3FYT_F Chain F, Acetyl xylan esterase [Bacillus pumilus],3FYT_G Chain G, Acetyl xylan esterase [Bacillus pumilus],3FYT_H Chain H, Acetyl xylan esterase [Bacillus pumilus],3FYT_I Chain I, Acetyl xylan esterase [Bacillus pumilus],3FYT_L Chain L, Acetyl xylan esterase [Bacillus pumilus],3FYT_M Chain M, Acetyl xylan esterase [Bacillus pumilus],3FYT_N Chain N, Acetyl xylan esterase [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 5.59e-99 26 429 35 437
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
P94388 7.66e-34 131 412 9 298
Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2 3.62e-21 131 412 9 303
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
0.001015 0.992186 0.006051 0.000259 0.000236 0.000229

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003572_01211.