CAZyme Information: FOZG_04431-t36_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOZG_04431-t36_1-p1
• CAZy Family: CBM50|CBM50
• CAZyme Description: alpha-glucosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
324		37061.57	4.5784

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FoxysporumFo47	18556	660027	365	18191

• Gene Location: location=JH717897.1:5364892-5365892(-)

Full Sequence      

MSPMELSKIASALYKRFMTEECESSSTWLSITPPINTLGLSTYDPLLRTQSKISTFGGSQ
RPNNWRSQFTKPAWTFDDTTQEYYIHVYASGQPDLNWENEACRREIYDNAIKFWFDRGVD
GFRVDTDNKFSKVSGLPDAPIVEPDQETQTAVCHYANGPRIHEYLYEMKQVLAPYDIMTV
GELPNTPDLEDMWKYISPNSQPGPQEIDMVFNFDTVNLGQTPGNRFLPIPFDNDFKRCLT
KWQKLPETTGAWTTVFLENHDQGRSVSRFGSDLPEFREQVAKMLASLLATMTGTLFLYQG
QEIGLINGPESWSANEYKCVRSVN

Enzyme Prediction     

EC	3.2.1.10:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	51	307	2e-96	0.7075208913649025

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200472	AmyAc_SI_OligoGlu_DGase	2.04e-111	60	317	129	384	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	1.20e-70	62	324	131	380	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.
395077	Alpha-amylase	2.39e-67	57	309	105	332	Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.
182849	PRK10933	8.66e-61	62	324	138	386	trehalose-6-phosphate hydrolase; Provisional
200471	AmyAc_OligoGlu_TS	1.15e-49	57	310	133	387	Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), trehalose synthase (also called maltose alpha-D-glucosyltransferase), and related proteins. 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. Trehalose synthase (EC 5.4.99.16) catalyzes the isomerization of maltose to produce trehalulose. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD50433.1|GH13_40	5.24e-190	68	317	95	344
QKX63079.1|GH13_40	1.64e-93	57	324	141	407
SJX62703.1|GH13_40	6.82e-93	51	324	145	415
BCS21116.1|GH13_40	8.76e-93	51	324	136	409
CBQ72869.1|GH13_40	1.91e-92	51	324	145	415

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7P01_A	1.25e-73	51	324	142	412	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]
3A47_A	1.46e-72	62	324	152	414	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	1.12e-71	62	324	152	414	Crystal structure of isomaltase in complex with isomaltose [Saccharomyces cerevisiae],3AXI_A Crystal structure of isomaltase in complex with maltose [Saccharomyces cerevisiae]
1UOK_A	1.04e-62	60	324	135	390	Crystal Structure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]
4MAZ_A	1.55e-62	62	307	137	377	The Structure of MalL mutant enzyme V200S from Bacillus subtilus [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q02751|MALT_CANAX	6.08e-89	52	324	133	401	Alpha-glucosidase OS=Candida albicans OX=5476 GN=MAL2 PE=1 SV=4
sp|P40884|IMA5_YEAST	2.76e-74	62	320	147	405	Oligo-1,6-glucosidase IMA5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA5 PE=2 SV=1
sp|P53051|MALX3_YEAST	7.51e-72	62	324	152	414	Oligo-1,6-glucosidase IMA1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA1 PE=1 SV=1
sp|Q08295|IMA2_YEAST	6.15e-70	62	324	152	414	Oligo-1,6-glucosidase IMA2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA2 PE=2 SV=1
sp|Q9P6J3|MALT_SCHPO	6.99e-70	62	324	150	409	Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mal1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FOZG_04431-t36_1-p1.