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CAZyme Information: MGYG000001548_03820

You are here: Home > Sequence: MGYG000001548_03820

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 Paenibacillus_A tuaregi
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_A; Paenibacillus_A tuaregi
CAZyme ID MGYG000001548_03820
CAZy Family CE7
CAZyme Description Cephalosporin-C deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
320 MGYG000001548_4|CGC70 36401.33 5.2511
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001548 5663842 Isolate not provided not provided
Gene Location Start: 4191385;  End: 4192347  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.1.1.72 3.1.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
CE7 3 312 4.2e-111 0.9712460063897763

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam05448 AXE1 6.12e-134 3 318 3 315
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-121 3 320 4 317
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506 DAP2 6.67e-15 57 305 367 596
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
pfam12146 Hydrolase_4 1.74e-08 86 304 7 231
Serine aminopeptidase, S33. This domain is found in bacteria and eukaryotes and is approximately 110 amino acids in length. It is found in association with pfam00561. The majority of the members in this family carry the exopeptidase active-site residues of Ser-122, Asp-239 and His-269 as in UniProtKB:Q7ZWC2.
pfam00326 Peptidase_S9 2.02e-07 106 303 11 187
Prolyl oligopeptidase family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AFH61480.1 9.11e-186 1 320 1 319
AFC29301.1 9.11e-186 1 320 1 319
AEI40688.1 1.31e-185 1 320 11 329
AIQ16866.1 1.91e-185 1 320 1 320
AIQ67834.1 1.82e-183 1 320 1 320

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3FCY_A 1.25e-122 3 320 30 344
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]
7CUZ_A 2.66e-101 7 311 4 306
ChainA, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_B Chain B, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_C Chain C, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147],7CUZ_D Chain D, Acetylxylan esterase [Lactococcus lactis subsp. lactis KF147]
6AGQ_A 1.31e-62 4 308 5 308
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 4.92e-55 3 307 4 302
structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
3FVR_A 5.19e-55 3 307 4 302
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
P94388 1.36e-54 3 307 4 302
Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2 1.14e-42 3 304 4 304
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 4.64e-23 6 297 132 414
Acetyl esterase Axe7A OS=Prevotella ruminicola (strain ATCC 19189 / JCM 8958 / 23) OX=264731 GN=axe7A 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
1.000036 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001548_03820.