CAZyme Information: ASPFODRAFT_391272-t33_1-p1

Basic Information

• Species: Aspergillus luchuensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis
• CAZyme ID: ASPFODRAFT_391272-t33_1-p1
• CAZy Family: GH31
• CAZyme Description: carbohydrate-binding module family 13 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
538		59231.03	4.4482

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AluchuensisCBS106.47	13784	1137211	282	13502

• Gene Location: location=KV878251:721622-723238(-)

Full Sequence      

MNQGIKSILVAATLATMLPLQAYSSIERSSLLPTPPMGFNNWARFMCDLNETLFIETADA
MAANGLRDAGYNRINLDDCWMAYQRSDNGSLQWNTTKFPHGLPWLANYVKAKGFYFGIYE
DSGNMTCGGYPGSYKHEEQDANTFASWGIDYLKLDGCNVYATQGRTLEEEYKQRYGHWHQ
VLSNMQHSLIFSESAPAYFAGTDNNTDWYTVMDWVPIYGELARHSTDILVYSGAGSAWDS
IINNYNYNTLLARYQQPGYFNDPDFLIPDHPGLTANEKRSHFALWASFSAPLIISAYIPA
LSKDEIAFLTNEALIAVDQDPLAQQATLASRDDTLDILTRNLANGDRLLTVLNKGNATVT
REIPVQWLGLVNTGCTYTAEDLWNGDTHKIGDHIKVELASHATAVFRLSLPDECSSVVPT
GLIFNTASGNCLAATSDSSVAFQSCNGEDSQIWWVTSSGVISPLSQTTQCLTADGSSVKL
QACDSTEDDGQKWTYAVTGNLKNAKTDSCLTEGPVQMKSCLDERNGQVFGLPSGVQLS

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	386	2.9e-59	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	2.56e-112	35	320	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	2.48e-81	34	320	1	284	Alpha galactosidase A.
166449	PLN02808	1.07e-76	9	409	2	384	alpha-galactosidase
178295	PLN02692	2.45e-68	23	408	39	408	alpha-galactosidase
177874	PLN02229	7.88e-63	3	387	19	394	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAK44933.1|CBM13|GH27|3.2.1.49	0.0	1	538	1	537
CAA44950.1|CBM13|GH27|3.2.1.22	0.0	1	538	9	545
BCS13393.1|CBM13|GH27	0.0	17	538	1	490
AEQ39734.1|GH27|3.2.1.49	0.0	37	523	1	487
AAE69559.1|CBM13|GH27|3.2.1.22	1.39e-303	1	440	9	447

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UAS_A	2.30e-68	34	409	8	360	Chain A, alpha-galactosidase [Oryza sativa]
4OGZ_A	7.52e-62	31	366	96	432	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]
3LX9_A	2.01e-61	29	354	3	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]
1R46_A	3.52e-60	29	354	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]
1KTB_A	1.61e-59	29	396	3	372	The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus],1KTC_A The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P28351|AGALA_ASPNG	0.0	1	538	9	545	Alpha-galactosidase A OS=Aspergillus niger OX=5061 GN=aglA PE=1 SV=1
sp|A2QL72|AGALA_ASPNC	0.0	1	538	1	537	Probable alpha-galactosidase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=aglA PE=3 SV=1
sp|Q4WVZ3|AGALA_ASPFU	1.83e-257	9	537	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|B8MWJ5|AGALA_ASPFN	5.61e-257	10	538	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
sp|Q2UT06|AGALA_ASPOR	4.58e-256	10	538	10	533	Probable alpha-galactosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 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 ASPFODRAFT_391272-t33_1-p1.