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CAZyme Information: ATEG_04382-t26_1-p1

You are here: Home > Sequence: ATEG_04382-t26_1-p1

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 Aspergillus terreus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus terreus
CAZyme ID ATEG_04382-t26_1-p1
CAZy Family GH18
CAZyme Description alpha-galactosidase A precursor
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
805 89493.80 5.0616
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AterreusNIH2624 10551 341663 150 10401
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.49:3 3.2.1.22:2 3.2.1.49:2 3.2.1.22:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH27 124 381 2.7e-54 0.9868995633187773

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
269893 GH27 1.63e-104 30 315 1 271
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 1.72e-79 4 403 1 384
alpha-galactosidase
178295 PLN02692 4.68e-77 29 400 55 406
alpha-galactosidase
374582 Melibiase_2 1.41e-75 29 315 1 284
Alpha galactosidase A.
177874 PLN02229 1.33e-60 23 403 56 418
alpha-galactosidase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.12e-244 8 523 8 529
2.88e-242 16 523 4 512
2.88e-242 16 523 4 512
3.76e-242 8 523 8 529
3.04e-241 8 523 8 529

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.26e-62 29 403 8 360
Chain A, alpha-galactosidase [Oryza sativa]
4.02e-60 26 349 96 420
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]
4.51e-57 26 379 5 358
The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus],1KTC_A The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus]
1.50e-55 26 349 5 325
Chain A, Alpha-galactosidase A [Homo sapiens],3LX9_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXA_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXA_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXB_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXB_B Chain B, Alpha-galactosidase A [Homo sapiens],3LXC_A Chain A, Alpha-galactosidase A [Homo sapiens],3LXC_B Chain B, Alpha-galactosidase A [Homo sapiens]
2.29e-54 26 349 5 325
Structure of human alpha-galactosidase [Homo sapiens],1R46_B Structure of human alpha-galactosidase [Homo sapiens],1R47_A Structure of human alpha-galactosidase [Homo sapiens],1R47_B Structure of human alpha-galactosidase [Homo sapiens],3GXN_A Crystal structure of apo alpha-galactosidase A at pH 4.5 [Homo sapiens],3GXN_B Crystal structure of apo alpha-galactosidase A at pH 4.5 [Homo sapiens],3GXP_A Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 [Homo sapiens],3GXP_B Crystal structure of acid-alpha-galactosidase A complexed with galactose at pH 4.5 [Homo sapiens],3GXT_A Crystal structure of alpha-galactosidase A at pH 4.5 complexed with 1-deoxygalactonijirimycin [Homo sapiens],3GXT_B Crystal structure of alpha-galactosidase A at pH 4.5 complexed with 1-deoxygalactonijirimycin [Homo sapiens],3HG2_A Human alpha-galactosidase catalytic mechanism 1. Empty active site [Homo sapiens],3HG2_B Human alpha-galactosidase catalytic mechanism 1. Empty active site [Homo sapiens],3HG4_A Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate [Homo sapiens],3HG4_B Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate [Homo sapiens],3HG5_A Human alpha-galactosidase catalytic mechanism 4. Product bound [Homo sapiens],3HG5_B Human alpha-galactosidase catalytic mechanism 4. Product bound [Homo sapiens],3S5Y_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Y_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Z_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3S5Z_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],4NXS_A Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT [Homo sapiens],4NXS_B Crystal structure of human alpha-galactosidase A in complex with 1-deoxygalactonojirimycin-pFPhT [Homo sapiens],6IBK_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfamidate ME763 [Homo sapiens],6IBK_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfamidate ME763 [Homo sapiens],6IBM_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfate ME776 [Homo sapiens],6IBM_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclosulfate ME776 [Homo sapiens],6IBR_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol epoxide LWA481 [Homo sapiens],6IBR_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol epoxide LWA481 [Homo sapiens],6IBT_A Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol aziridine ME737 [Homo sapiens],6IBT_B Crystal structure of human alpha-galactosidase A in complex with alpha-galactose configured cyclophellitol aziridine ME737 [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 1 523 1 523
Probable alpha-galactosidase A OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=aglA PE=3 SV=2
6.68e-243 8 523 8 529
Probable alpha-galactosidase A OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=aglA PE=3 SV=1
5.41e-242 8 523 8 529
Probable alpha-galactosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglA PE=3 SV=1
7.93e-237 2 525 14 543
Alpha-galactosidase A OS=Aspergillus niger OX=5061 GN=aglA PE=1 SV=1
2.06e-232 2 525 6 535
Probable alpha-galactosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.001198 0.998781 CS pos: 19-20. Pr: 0.9433

TMHMM  Annotations      help

There is no transmembrane helices in ATEG_04382-t26_1-p1.