CAZyme Information: FOXG_07431-t26_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOXG_07431-t26_1-p1
• CAZy Family: CE8|CE8|CE8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
589	CM000592.1|CGC21	67524.55	5.9465

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum4287	21354	426428	429	20925

• Gene Location: location=CM000592.1:169748-171856(+)

Full Sequence      

MTQIYPASFLDTDSNGVGNINGITAKLDYLKELGVDILWISPGKTYLIHSGASNLTPAIS
LRKSTEGHGSNYRDIHRPYGTMQDVHHLIDELKARDMKLIMDLVFNHTSTQHPWFIDSAS
SAVSARRDWYIWRKPKYDVQGNRQPPNNWCSLFDETESAWTYDSQTDEYYLSLFSPFQAD
LNWETPFVREEVCDILRFWLDKGVSGFRMDVINLISKDQRFPDAEIRHPGRKYQPGECYF
ANGIRLMDYLQEMKTAVFSKYDTLTVGEMPYLVDEEERLKMVAAEEGVLNMIFTFEMIGL
DIVPEKGRFSNKPWKVSDLKNIIAKAYKLVNQDGWHTLFCENHDQPRSVTRFCDDSDEHR
VAGTKLLSIMQTSLPGTLYVYQGEELGMRNVPKSWALEEYIDIESVSYIKNVCSQFAEGS
PERKEAKNLLRLKARDNARTPMQWDSTSNGGFCPAGVKPWMRVNDDYTIVNAALQTSAGR
ANDRTMLLSPYRFWQRSIETRKKYKDLLVYGDLEIIDGTHPNVFAYKRISESKHSVTILN
FSKDEVKFTFPDGQGVTCWALGSYDALSMEKPKSGVIQLLPWEGLLGIA

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	18	391	4.6e-145	0.9972144846796658

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200472	AmyAc_SI_OligoGlu_DGase	0.0	3	503	7	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.
182849	PRK10933	4.28e-142	3	585	15	546	trehalose-6-phosphate hydrolase; Provisional
200470	AmyAc_OligoGlu_like	2.40e-117	3	492	10	434	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.
223443	AmyA	5.65e-109	3	551	5	493	Glycosidase [Carbohydrate transport and metabolism].
395077	Alpha-amylase	4.51e-107	18	392	1	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD50347.1|GH13_40	0.0	3	589	21	607
ABY89282.1|GH13_40	0.0	3	589	71	643
QRC97393.1|GH13_40	9.67e-215	3	588	25	599
CAE7200722.1|GH13_40	5.54e-213	3	588	27	596
SMR42775.1|GH13_40	3.16e-210	3	589	20	598

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7P01_A	9.76e-136	3	580	24	573	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	2.37e-129	3	552	13	521	Crystal Structure Of B. Cereus Oligo-1,6-Glucosidase [Bacillus cereus]
3A47_A	1.18e-125	3	589	22	588	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	9.33e-125	3	589	22	588	Crystal structure of isomaltase in complex with isomaltose [Saccharomyces cerevisiae],3AXI_A Crystal structure of isomaltase in complex with maltose [Saccharomyces cerevisiae]
4M56_A	1.57e-121	3	589	12	560	The Structure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168],4M56_B The Structure of Wild-type MalL from Bacillus subtilis [Bacillus subtilis subsp. subtilis str. 168]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9P6J3|MALT_SCHPO	1.58e-163	3	586	21	576	Alpha-glucosidase OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mal1 PE=2 SV=1
sp|P29094|O16G_PARTM	4.82e-144	3	583	13	553	Oligo-1,6-glucosidase OS=Parageobacillus thermoglucosidasius OX=1426 GN=malL PE=1 SV=1
sp|Q02751|MALT_CANAX	4.46e-138	3	548	14	536	Alpha-glucosidase OS=Candida albicans OX=5476 GN=MAL2 PE=1 SV=4
sp|Q08295|IMA2_YEAST	3.94e-129	3	589	22	588	Oligo-1,6-glucosidase IMA2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=IMA2 PE=2 SV=1
sp|P21332|O16G_BACCE	1.22e-128	3	552	13	521	Oligo-1,6-glucosidase OS=Bacillus cereus OX=1396 GN=malL PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000056	0.000001

TMHMM  Annotations     

There is no transmembrane helices in FOXG_07431-t26_1-p1.