CAZyme Information: FFUJ_00201-t31_1-p1

Basic Information

• Species: Fusarium fujikuroi
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium fujikuroi
• CAZyme ID: FFUJ_00201-t31_1-p1
• CAZy Family: AA11
• CAZyme Description: probable alpha-glucosidase (maltase)

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
613		70457.61	6.4271

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FfujikuroiIMI58289	15099	1279085	286	14813

• Gene Location: location=HF679023:6003674-6005572(+)

Full Sequence      

MHSVFPKVDRAPWREASVYQIYPSSFKDSNGDGIGDIQGIISELDYIKSLGVDMVWLSPV
LASPQIDMGYDISDYKDIYPPYGTMADHDSLIQSLHDRGLKYILDLVVNHTSDQHPWFKE
ARSSKNSRYRNWYFWRPARRDPKTGKRIPPNNWESFFSTSAWTWDDTTQEYYLHLWSSGQ
PDLNWENPEVVAAVHDIIRFWLDRGVDGFRMDVINYISKTPGLPDARIKKPGFLQKPTEH
CACGPRLHEYLRGIGSILREYNAFSVGEMPDADPEEVLKAVGQNRGELAMAFHFDIDGLD
LGTDHRFDPAVFQPTALKNVVNRWQTFMASNSGWNALHMENHDESRIVSRYASDSPPMRT
ISAKMLANHLAFQSGTLFIYQGQELAMVNLPREWGMDKYKDIECLNHWTLVQSYYQDDVK
KQKMYRERYRQVGRDNARTPMQWNSESPYAGFMLNGSTRAEPWMSIHPDFATWNVSNMLA
DSQSSLNHWRSVLRFRKKHVDILVYGGFEMLNMDIEEDVIAYIRTDGTADESSHRPTKVL
VVTSFSGSDICWTIPSKARDILLDMSADSGKPIINMKGLVTALGNYEGVNELTMKEGKHA
IRLRPYQTLIAMI

Enzyme Prediction     

EC	5.4.99.11:5	3.2.1.20:4	3.2.1.10:1	3.2.1.-:1	3.2.1.70:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	35	390	5.7e-153	0.9972144846796658

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200472	AmyAc_SI_OligoGlu_DGase	0.0	14	498	1	428	Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
274115	trehalose_treC	1.27e-176	13	610	2	540	alpha,alpha-phosphotrehalase. Trehalose is a glucose disaccharide that serves in many biological systems as a compatible solute for protection against hyperosmotic and thermal stress. This family describes trehalose-6-phosphate hydrolase, product of the treC (or treA) gene, which is often found together with a trehalose uptake transporter and a trehalose operon repressor.
200469	AmyAc_OligoGlu	1.17e-145	13	519	3	471	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
200470	AmyAc_OligoGlu_like	1.85e-145	13	499	3	443	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
182849	PRK10933	1.50e-141	13	511	8	480	trehalose-6-phosphate hydrolase; Provisional

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QGI76837.1|GH13_40	0.0	1	613	1	613
QGI59637.1|GH13_40	0.0	1	613	1	613
CCT63178.1|GH13_40	0.0	1	613	1	613
QGI90549.1|GH13_40	0.0	1	613	1	613
QKD60697.1|GH13_40	6.17e-223	3	613	22	595

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7P01_A	4.07e-167	13	514	17	514	Chain A, BaAG2 [Blastobotrys adeninivorans],7P01_B Chain B, BaAG2 [Blastobotrys adeninivorans],7P07_A Chain A, BaAG2 [Blastobotrys adeninivorans],7P07_B Chain B, BaAG2 [Blastobotrys adeninivorans]
1UOK_A	6.07e-154	13	555	6	520	Crystal Structure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]
3A47_A	4.25e-145	3	514	5	521	Crystal structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae],3A4A_A Crystal structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae],3AJ7_A Crystal Structure of isomaltase from Saccharomyces cerevisiae [Saccharomyces cerevisiae]
3AXH_A	3.38e-144	3	514	5	521	Crystal structure of isomaltase in complex with isomaltose [Saccharomyces cerevisiae],3AXI_A Crystal structure of isomaltase in complex with maltose [Saccharomyces cerevisiae]
5DO8_A	1.05e-139	13	524	7	495	1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_B 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e],5DO8_C 1.8 Angstrom crystal structure of Listeria monocytogenes Lmo0184 alpha-1,6-glucosidase [Listeria monocytogenes EGD-e]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9P6J3|MALT_SCHPO	8.77e-196	13	568	14	559	Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mal1 PE=2 SV=1
sp|P29094|O16G_PARTM	9.57e-159	8	613	1	559	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
sp|Q02751|MALT_CANAX	3.97e-157	13	569	7	555	Alpha-glucosidase OS=Candida albicans OX=5476 GN=MAL2 PE=1 SV=4
sp|P21332|O16G_BACCE	3.12e-153	13	555	6	520	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1
sp|Q08295|IMA2_YEAST	1.38e-145	3	564	5	562	Oligo-1,6-glucosidase IMA2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000026	0.000004

TMHMM  Annotations     

There is no transmembrane helices in FFUJ_00201-t31_1-p1.