CAZyme Information: KIS69778.1

Basic Information

• Species: Ustilago maydis
• Lineage: Basidiomycota; Ustilaginomycetes; ; Ustilaginaceae; Ustilago; Ustilago maydis
• CAZyme ID: KIS69778.1
• CAZy Family: GH5
• CAZyme Description: putative alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
536	CM003144|CGC4	60888.74	5.2954

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Umaydis521	6910	237631	145	6765

• Gene Location: location=CM003144:785481-787091(+)

Full Sequence      

MASSANKHADKHEHNYTMMQAFEWYTQGEGKHWQWLGDNAKRFADMGITAVWIPPPTKGA
SASSTGYDIYDTWDLGEFAHPRDEKAGVKPPNRTKYGTREQLEKAMQELRKNGISIYVDA
VLNHRMGADELQTFKARMVDSNDRTKFCSDPYDIQGWTKFTFPGRKDKYSDFKWGFEHFA
GVDWDQKSDTKAIFRIEGDGKSWATDVDKENGNYSFLMGADIDHSHPDAKRDLLNWGAWI
MRNFPVAGFRFDAVKHISREFIHDFVKHIREEARKLREERGLEPADESEGPIAFSVGEFW
KDSLGSCLEYLGKFGDEQFSLFDAPLHYNFKEAGDGAESYDLRKIFDDTVVQARPIDAVT
LVDNHDTQQGQALESTVPAQFKPLAYSLILMRIDGYPCVFLGDLDGCNPTGIDNGEGKAD
PMADLEKFVKARKYYAYGEQKDVWDHPNCVAWVRTGTKADDGSGYDASVTIICNGSAQGT
KWVEVGKRYAGQNFVDVIGWFQGQAKVNEDGWVEVHCHPRSASIWVPEDSKHREFF

Enzyme Prediction     

EC	3.2.1.1:2	3.2.1.116:1	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	43	406	2.6e-141	0.9912280701754386

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
236518	PRK09441	0.0	13	526	1	479	cytoplasmic alpha-amylase; Reviewed
200457	AmyAc_bac_fung_AmyA	0.0	15	434	1	391	Alpha amylase catalytic domain found in bacterial and fungal Alpha amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes bacterial and fungal proteins. 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.
200453	AmyAc_arch_bac_plant_AmyA	1.10e-40	18	401	2	272	Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. 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.
215419	PLN02784	3.62e-18	18	304	505	703	alpha-amylase
395077	Alpha-amylase	2.74e-16	45	403	15	324	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
SJX66056.1|GH13_5	0.0	1	536	1	536
CBQ71030.1|GH13_5	0.0	1	536	1	536
CDI56403.1|GH13_5	0.0	1	536	1	537
CDU23082.1|GH13_5	0.0	1	536	1	536
SAM62792.1|GH13_5	2.36e-317	1	536	1	484

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1W9X_A	1.64e-146	15	526	2	479	Chain A, Alpha Amylase [Sutcliffiella halmapala]
2GJP_A	1.88e-146	15	526	6	483	Chain A, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]
1WP6_A	5.32e-146	15	526	6	483	Crystal structure of maltohexaose-producing amylase from alkalophilic Bacillus sp.707. [Bacillus sp. 707],1WPC_A Crystal structure of maltohexaose-producing amylase complexed with pseudo-maltononaose [Bacillus sp. 707],2D3L_A Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose. [Bacillus sp. 707],2D3N_A Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltohexaose [Bacillus sp. 707]
2DIE_A	3.13e-142	15	528	6	485	Alkaline alpha-amylase AmyK from Bacillus sp. KSM-1378 [Bacillus sp. (in: Bacteria)]
3BH4_A	7.58e-140	15	526	2	481	High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens],3BH4_B High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P19571|AMT6_BACS7	8.04e-145	15	526	39	516	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P00692|AMY_BACAM	1.06e-138	15	526	33	512	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P06278|AMY_BACLI	3.61e-136	15	526	33	510	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P06279|AMY_GEOSE	2.61e-134	15	527	39	516	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P26612|AMY2_ECOLI	7.20e-117	15	529	3	493	Cytoplasmic alpha-amylase OS=Escherichia coli (strain K12) OX=83333 GN=amyA PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999728	0.000305

TMHMM  Annotations     

There is no transmembrane helices in KIS69778.1.