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CAZyme Information: MGYG000003237_02412

You are here: Home > Sequence: MGYG000003237_02412

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 Victivallis sp002998355
Lineage Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; Victivallis; Victivallis sp002998355
CAZyme ID MGYG000003237_02412
CAZy Family CE7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
415 MGYG000003237_65|CGC3 45359.89 8.0518
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003237 4618450 MAG United States North America
Gene Location Start: 87680;  End: 88927  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000003237_02412.

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 133 405 5.4e-55 0.9105431309904153

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam05448 AXE1 9.63e-32 133 404 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 1.22e-26 133 392 19 291
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG0412 DLH 4.28e-04 238 402 60 203
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506 DAP2 0.006 247 388 435 579
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AVM46416.1 3.49e-309 1 415 1 415
SDU24469.1 2.79e-152 18 408 15 410
AHF91279.1 7.88e-133 1 411 1 428
AHF90182.1 4.44e-131 16 414 16 416
AVM46415.1 9.71e-123 20 415 74 470

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1L7A_A 1.29e-21 135 404 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 1.77e-21 135 404 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 3.29e-21 135 404 21 302
cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis]
5GMA_A 5.00e-20 136 392 34 307
Crystalstructure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_B Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_C Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_D Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_E Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8],5GMA_F Crystal structure of the P228A variant of Thermotoga maritima acetyl esterase [Thermotoga maritima MSB8]
3M81_A 5.00e-20 136 392 34 307
Crystalstructure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_B Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_C Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_D Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_E Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],3M81_F Crystal structure of Acetyl xylan esterase (TM0077) from THERMOTOGA MARITIMA at 2.50 A resolution (native apo structure) [Thermotoga maritima],5FDF_A Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_B Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_C Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_D Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_E Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5FDF_F Crystal structure of the monoclinic form of Thermotoga maritima Acetyl Esterase TM0077 (apo structure) at 1.76 Angstrom resolution [Thermotoga maritima],5JIB_A Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_B Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_C Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_D Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_E Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8],5JIB_F Crystal structure of the Thermotoga maritima acetyl esterase (TM0077) complex with a substrate analog [Thermotoga maritima MSB8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
D5EXI2 8.12e-36 135 391 143 411
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A PE=1 SV=1
P94388 7.09e-21 135 404 21 302
Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2 2.35e-19 136 392 22 295
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
0.000239 0.999104 0.000188 0.000159 0.000141 0.000143

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003237_02412.