CAZyme Information: AKAW_06210-t41_1-p1

Basic Information

• Species: Aspergillus luchuensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
• CAZyme ID: AKAW_06210-t41_1-p1
• CAZy Family: GH28
• CAZyme Description: alpha-galactosidase (AglA)

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
506	DF126461|CGC2	55337.90	4.5599

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AluchuensisIFO4308	11755	1033177	267	11488

• Gene Location: location=DF126461:653292-654906(-)

Full Sequence      

MNQGIKSILVAATLATMLPLQAYSSIERSSLLPTPPMGFNNWARFMCDLNETLFIETADA
MAANGLRDAGYNRINLDDCWMAYQRSDNGSLQWNTTKFPHGLPWLANYVKAKGFYFGIYE
DSGNMTCGGYPGSYKHEEQDANTFASWGIDYLKLDGCNVYATQGRTLEEEYKQRYGHWHQ
VQQYAALTDLLRVSPGILCGGAGSAWDSIINNYNYNTLLARYQQPGYFNDPDFLIPDHPG
LTANEKRSHFALWASFSAPLIISAYIPALSKDEIAFLTNEALIAVDQDPLAQQATLASRD
DTLDILTRNLANGDRLLTVLNKGNATVTRGIPVQWLGLVNTGCTYTVEDLWNGDTQKIGD
HIKVELASHATAVFRLSLPDECSSVVPTGLIFNTASGNCLAATSNSSVAFQSCNGEDSQI
WRVTSSGVISPLSQTTQCLTADGSSVKLQACDSTEDDGQKWTYAVTGNLKNAKTDSCLTE
GPVQMKSCLDERDGQVFGLPSGVQLS

Enzyme Prediction     

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

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	129	355	7.2e-52	0.9868995633187773

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	5.02e-106	35	288	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.
374582	Melibiase_2	4.50e-76	34	288	1	284	Alpha galactosidase A.
166449	PLN02808	2.43e-74	9	377	2	384	alpha-galactosidase
178295	PLN02692	3.45e-69	23	376	39	408	alpha-galactosidase
177874	PLN02229	2.39e-63	3	355	19	394	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS13393.1|CBM13|GH27	0.0	17	506	1	490
CAK44933.1|CBM13|GH27|3.2.1.49	0.0	1	506	1	537
CAA44950.1|CBM13|GH27|3.2.1.22	0.0	1	506	9	545
AEQ39734.1|GH27|3.2.1.49	3.13e-297	37	491	1	487
AAE69559.1|CBM13|GH27|3.2.1.22	3.25e-259	1	408	9	447

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UAS_A	1.13e-67	34	377	8	360	Chain A, alpha-galactosidase [Oryza sativa]
4OGZ_A	7.50e-60	31	382	96	467	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]
4NZJ_A	6.44e-57	31	328	96	426	Crystal structure of a putative alpha-galactosidase (BF1418) from Bacteroides fragilis NCTC 9343 at 1.57 A resolution [Bacteroides fragilis NCTC 9343]
1KTB_A	3.53e-55	29	364	3	372	The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus],1KTC_A The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus]
1R46_A	5.81e-55	29	322	3	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A2QL72|AGALA_ASPNC	0.0	1	506	1	537	Probable alpha-galactosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglA PE=3 SV=1
sp|P28351|AGALA_ASPNG	0.0	1	506	9	545	Alpha-galactosidase A OS=Aspergillus niger OX=5061 GN=aglA PE=1 SV=1
sp|Q4WVZ3|AGALA_ASPFU	2.90e-224	9	505	7	529	Probable alpha-galactosidase A OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=aglA PE=3 SV=1
sp|A1DDD8|AGALA_NEOFI	7.81e-222	9	505	7	529	Probable alpha-galactosidase A OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=aglA PE=3 SV=1
sp|B8MWJ5|AGALA_ASPFN	9.11e-219	10	506	10	533	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000285	0.999685	CS pos: 24-25. Pr: 0.9472

TMHMM  Annotations     

There is no transmembrane helices in AKAW_06210-t41_1-p1.