CAZyme Information: MELLADRAFT_74184-t26_1-p1

Basic Information

• Species: Melampsora larici-populina
• Lineage: Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina
• CAZyme ID: MELLADRAFT_74184-t26_1-p1
• CAZy Family: GH5
• CAZyme Description: family 13 glycoside hydrolase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
514		58985.59	5.1057

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Mlarici-populina98AG31	16380	747676	8	16372

• Gene Location: location=GL883094:1239925-1242861(+)

Full Sequence      

MADRANNFFHRERHGDEPPSHNYTMIQAFEWHSEGNGKHWKWFKDRVKHLADLGITAAWL
PPPTKASSMEGNGYDIYDLFDLGEFPNKEDPKKTRTKWGTKEELVDAVRQARECGVAVYI
DAVLNHKAGADFSETCKAKEVNSNNRNEEISDAYEIEAWTGFNFPQRKGKYSEFEWHSHH
FTGVDYDNKNKKKAIFKIEGNGKAWATDVDEENGNFDYLMFSDLDHSHPEVSDECKKWGI
WIIKELGAAGFRFDAVKHMDRGFVADFIKHVRREVGNPDLFAVGEFWKDDIDTISAYLEG
LDAQFSVFDAPLHYNFKKASDEGENYDIRQIFDDTLVQCRPVDAVTMVDNHDTQPYEALE
SWVGPQFKPLAYSIILLRPDGYPCVFLGDLEGIKGEHKFEPMSQLDDLIRARKLFAYGPM
KDYWDHERCAGWVRDGDERHDGCAVVISNGGEGTKRMEVGRNHSGEEWTDCLGWHPDTIC
IGEDGWAEFKCPASSVSVWTKKDAKGRDEYKRKA

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	49	393	2.4e-147	0.9970760233918129

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
236518	PRK09441	0.0	22	499	3	478	cytoplasmic alpha-amylase; Reviewed
200457	AmyAc_bac_fung_AmyA	0.0	22	414	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	1.47e-46	25	416	2	295	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	1.24e-21	25	413	505	833	alpha-amylase
395077	Alpha-amylase	1.64e-20	45	389	8	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
AFX74688.1|GH13_5	7.28e-250	22	510	40	526
QRV94121.1|GH13_5	5.00e-241	1	510	1	505
CDZ98132.1|GH13_5	1.55e-240	22	512	73	561
QRW21587.1|GH13_5	3.94e-240	1	512	1	509
QRV79482.1|GH13_5	1.66e-239	1	510	1	505

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1W9X_A	5.66e-165	22	502	2	481	Chain A, Alpha Amylase [Sutcliffiella halmapala]
2GJP_A	6.48e-165	22	502	6	485	Chain A, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]
3BH4_A	2.44e-164	22	502	2	483	High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens],3BH4_B High resolution crystal structure of Bacillus amyloliquefaciens alpha-amylase [Bacillus amyloliquefaciens]
1WP6_A	7.42e-164	22	502	6	485	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]
1E3X_A	1.97e-163	22	502	2	483	Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.92A [Bacillus amyloliquefaciens],1E3Z_A Acarbose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.93A [Bacillus amyloliquefaciens],1E40_A Tris/maltotriose complex of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 2.2A [Bacillus amyloliquefaciens],1E43_A Native structure of chimaeric amylase from B. amyloliquefaciens and B. licheniformis at 1.7A [Bacillus amyloliquefaciens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P00692|AMY_BACAM	3.56e-163	22	502	33	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P19571|AMT6_BACS7	1.16e-162	22	502	39	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P06279|AMY_GEOSE	1.77e-156	22	499	39	514	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P06278|AMY_BACLI	5.50e-154	22	502	33	512	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P26613|AMY2_SALTY	6.40e-132	22	503	3	493	Cytoplasmic alpha-amylase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) OX=99287 GN=amyA PE=3 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000045	0.000003

TMHMM  Annotations     

There is no transmembrane helices in MELLADRAFT_74184-t26_1-p1.