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CAZyme Information: KRZ98399.1

You are here: Home > Sequence: KRZ98399.1

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 Debaryomyces fabryi
Lineage Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Debaryomyces; Debaryomyces fabryi
CAZyme ID KRZ98399.1
CAZy Family AA1
CAZyme Description Alpha-galactosidase [Source:UniProtKB/TrEMBL;Acc:A0A0V1PQG1]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
348 LMYN01000299|CGC1 39025.38 4.4799
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_DfabryiCBS789 6025 N/A 0 6025
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.22:15

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 55 320 8.4e-75 0.9737991266375546

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 2.41e-112 1 250 42 271
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.
166449 PLN02808 2.80e-89 1 345 73 384
alpha-galactosidase
177874 PLN02229 3.76e-84 1 347 104 420
alpha-galactosidase
178295 PLN02692 4.26e-84 1 348 97 412
alpha-galactosidase
374582 Melibiase_2 9.39e-65 1 250 53 284
Alpha galactosidase A.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.32e-252 1 348 70 417
1.64e-146 1 346 74 420
1.64e-146 1 346 74 420
1.08e-137 1 347 70 426
3.08e-137 1 347 70 426

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.13e-128 1 347 50 393
Crystal structure of alpha-galactosidase I from Mortierella vinacea [Umbelopsis vinacea]
2.58e-107 1 321 71 399
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRL_A Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae]
4.12e-106 1 321 71 399
Chain A, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_B Chain B, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_C Chain C, Alpha-galactosidase 1 [Saccharomyces cerevisiae],3LRM_D Chain D, Alpha-galactosidase 1 [Saccharomyces cerevisiae]
3.67e-72 1 345 50 360
Chain A, alpha-galactosidase [Oryza sativa]
1.67e-70 1 345 50 361
Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.91e-147 1 346 74 420
Alpha-galactosidase mel1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mel1 PE=3 SV=1
2.20e-116 1 324 70 401
Alpha-galactosidase OS=Lachancea cidri OX=29831 GN=MEL PE=3 SV=1
3.57e-110 1 348 71 419
Alpha-galactosidase OS=Saccharomyces mikatae OX=114525 GN=MEL PE=3 SV=1
5.21e-107 1 304 71 379
Alpha-galactosidase OS=Saccharomyces pastorianus (strain ATCC 76529 / Carlsberg bottom yeast no.1 / CBS 1513 / CLIB 176 / NBRC 1167 / NCYC 396 / NRRL Y-12693) OX=1073566 GN=MEL PE=3 SV=1
7.37e-107 1 321 71 399
Alpha-galactosidase 1 OS=Saccharomyces cerevisiae OX=4932 GN=MEL1 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000048 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KRZ98399.1.