CAZyme Information: ASPCADRAFT_511328-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_511328-t33_1-p1
• CAZy Family: GT25
• CAZyme Description: carbohydrate-binding module family 13 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
544	KV907493|CGC22	59944.22	5.3825

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcarbonariusITEM5010	11735	602072	260	11475

• Gene Location: location=KV907493:138965-140599(+)

Full Sequence      

MGKVKNIMNCRTKGIFFAAALVAMFPQAYGSIERSSLLPTPPMGFNNWARFMCDLNETLF
TETADAMASNGLRDAGYNRINLDDCWMAYQRADNGSLQWNTTKFPHGLPWLGNYLKALGF
KFGIYEDSGNLTCGGYPGSYNHEELDANTFASWGIDYLKVDGCNVYATQGRTLEEEYKHR
YGHWHQVLSHMEHPLIFSESAPAYFAGTENRTDWYTVMDWVPVYGELARHSTDILVYSGA
GSAWDSIINNYNYNTLLARYQRPGYFNDPDFLIPDHPGLTADEKRSHFALWASFSAPLII
SAYIPALSKDEIAYLSNKALIAVDQDPLAQQATLASRDDTLDMLTRSLSNGDRLLTVLNR
GNKTVKTNIPIQWLGLTETGCTYTAEDLWDSSLQKIGSHITVQLATHATAVFRISLPQSC
STVIPTGLVFNTASGHCLTAGSNSSITFQPCNGQASQIWQVTSLGALRPISSTAQCLTAT
DDSVKLQACDNSGSDAQIWTYAVTGNLKHAKTGGCLTEDSVQLQRCLDETNSQVFGLPSG
VQLS

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	135	391	3.1e-58	0.9781659388646288

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	1.79e-114	41	326	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	3.88e-81	40	326	1	284	Alpha galactosidase A.
166449	PLN02808	1.64e-78	40	412	31	381	alpha-galactosidase
178295	PLN02692	1.06e-71	29	412	39	406	alpha-galactosidase
177874	PLN02229	6.96e-65	17	421	37	423	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAA44950.1|CBM13|GH27|3.2.1.22	0.0	4	544	5	545
CAK44933.1|CBM13|GH27|3.2.1.49	0.0	8	544	1	537
AEQ39734.1|GH27|3.2.1.49	0.0	43	529	1	487
BCS13393.1|CBM13|GH27	1.48e-294	27	544	5	490
AAE69559.1|CBM13|GH27|3.2.1.22	1.39e-293	4	446	5	447

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UAS_A	1.17e-65	40	407	8	352	Chain A, alpha-galactosidase [Oryza sativa]
4OGZ_A	1.62e-62	37	360	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]
3LX9_A	8.77e-61	35	360	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]
1KTB_A	4.80e-60	34	402	2	372	The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus],1KTC_A The Structure of alpha-N-Acetylgalactosaminidase [Gallus gallus]
1R46_A	1.53e-59	35	360	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	8	544	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	4	544	5	545	Alpha-galactosidase A OS=Aspergillus niger OX=5061 GN=aglA PE=1 SV=1
sp|B8MWJ5|AGALA_ASPFN	3.51e-257	8	544	1	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	2.86e-256	8	544	1	533	Probable alpha-galactosidase A OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=aglA PE=3 SV=1
sp|Q4WVZ3|AGALA_ASPFU	5.36e-256	21	543	12	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.003701	0.996260	CS pos: 30-31. Pr: 0.9532

TMHMM  Annotations     

Start	End
13	30