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CAZyme Information: MGYG000001507_01027

You are here: Home > Sequence: MGYG000001507_01027

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 ihuae
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus ihuae
CAZyme ID MGYG000001507_01027
CAZy Family CE7
CAZyme Description Cephalosporin-C deacetylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
319 MGYG000001507_1|CGC18 36102.92 4.9526
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001507 6631509 Isolate not provided not provided
Gene Location Start: 1107446;  End: 1108405  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 4 312 1.2e-111 0.9680511182108626

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam05448 AXE1 1.62e-135 5 314 6 312
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 1.21e-119 6 317 8 314
Cephalosporin-C deacetylase or related acetyl esterase [Secondary metabolites biosynthesis, transport and catabolism].
COG1506 DAP2 1.28e-13 56 306 367 598
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism].
pfam12146 Hydrolase_4 7.52e-07 85 303 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.
pfam01738 DLH 5.21e-06 78 207 8 128
Dienelactone hydrolase family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QSF47666.1 1.08e-226 1 304 2 305
AIQ16866.1 3.58e-215 2 319 3 320
AIQ60063.1 4.67e-211 1 319 1 320
AIQ31297.1 1.34e-210 1 319 1 320
AIQ47387.1 1.06e-209 1 319 1 319

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3FCY_A 3.00e-118 6 319 34 344
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 1.12e-102 10 310 8 306
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 5.70e-64 6 314 8 315
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 1.60e-59 6 306 8 302
structuralGenomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis],1L7A_B structural Genomics, crystal structure of Cephalosporin C deacetylase [Bacillus subtilis]
1ODT_C 2.26e-59 6 306 8 302
cephalosporinC deacetylase mutated, in complex with acetate [Bacillus subtilis],1ODT_H cephalosporin C deacetylase mutated, in complex with acetate [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P94388 4.41e-59 6 306 8 302
Cephalosporin-C deacetylase OS=Bacillus subtilis (strain 168) OX=224308 GN=cah PE=1 SV=1
Q9WXT2 3.46e-40 6 303 8 304
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 5.60e-25 13 296 137 414
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
1.000072 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001507_01027.