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CAZyme Information: KDQ27114.1

You are here: Home > Sequence: KDQ27114.1

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 Pleurotus ostreatus
Lineage Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
CAZyme ID KDQ27114.1
CAZy Family GH128
CAZyme Description glycoside hydrolase family 27 protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
454 48518.23 5.9712
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PostreatusPC15 12460 1137138 164 12296
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:58 2.4.1.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 99 350 6.6e-55 0.9868995633187773

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 1.60e-108 7 276 5 271
glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
178295 PLN02692 5.67e-80 7 374 60 408
alpha-galactosidase
177874 PLN02229 2.51e-78 7 385 67 423
alpha-galactosidase
166449 PLN02808 2.87e-77 7 375 36 384
alpha-galactosidase
374582 Melibiase_2 5.63e-61 7 276 6 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.20e-155 7 375 93 457
1.71e-151 7 362 63 418
3.05e-150 7 375 124 488
7.73e-141 16 374 48 385
3.69e-137 7 375 92 443

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.73e-116 7 374 16 410
Chain A, alpha-galactosidase [Trichoderma reesei],1T0O_A Chain A, alpha-galactosidase [Trichoderma reesei]
1.38e-72 7 367 13 383
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
6.77e-66 7 375 13 360
Chain A, alpha-galactosidase [Oryza sativa]
2.72e-65 7 276 13 272
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
1.05e-51 7 276 104 386
Crystal structure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343],4OGZ_B Crystal structure of a putative alpha-galactosidase/melibiase (BF4189) from Bacteroides fragilis NCTC 9343 at 2.00 A resolution [Bacteroides fragilis NCTC 9343]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.37e-112 7 374 38 444
Probable alpha-galactosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=aglB PE=3 SV=1
2.42e-110 7 376 39 450
Probable alpha-galactosidase B OS=Talaromyces emersonii OX=68825 PE=3 SV=1
1.61e-109 7 370 33 427
Probable alpha-galactosidase B OS=Penicillium simplicissimum OX=69488 GN=agl1 PE=2 SV=1
4.65e-108 7 376 31 441
Probable alpha-galactosidase B OS=Aspergillus niger OX=5061 GN=aglB PE=2 SV=1
4.65e-108 7 376 31 441
Probable alpha-galactosidase B OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000077 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KDQ27114.1.