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CAZyme Information: MGYG000000353_01639

You are here: Home > Sequence: MGYG000000353_01639

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 UBA7173 sp900548705
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp900548705
CAZyme ID MGYG000000353_01639
CAZy Family CE7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
432 48092.95 4.8007
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000353 2738445 MAG Sweden Europe
Gene Location Start: 11790;  End: 13088  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000353_01639.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 125 412 4.2e-67 0.9137380191693291

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam05448 AXE1 3.73e-52 130 408 21 299
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 5.42e-49 121 413 13 304
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
pfam00326 Peptidase_S9 2.36e-05 224 422 5 206
Prolyl oligopeptidase family.
COG1506 DAP2 2.77e-04 143 422 340 613
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
COG0412 DLH 0.002 182 383 12 174
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QUB71398.1 1.89e-130 25 422 262 661
SJX74200.1 1.79e-91 53 426 163 528
QIK58759.1 4.01e-85 37 426 205 586
QIK53342.1 6.11e-84 37 426 205 586
CBK67642.1 1.06e-82 78 422 84 421

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1L7A_A 3.84e-38 113 426 4 316
structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
1ODS_A 3.86e-37 113 422 4 312
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 5.37e-37 113 422 4 312
cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis]
3FVR_A 3.96e-34 129 421 21 311
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 1.05e-33 129 421 21 311
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
P94388 1.09e-36 113 422 4 312
Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
D5EXI2 2.09e-27 74 413 90 425
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
Q9WXT2 2.22e-25 129 408 21 303
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
0.000331 0.998978 0.000189 0.000184 0.000153 0.000148

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000353_01639.