CAZyme Information: QRC91644.1

Basic Information

• Species: Parastagonospora nodorum
• Lineage: Ascomycota; Dothideomycetes; ; Phaeosphaeriaceae; Parastagonospora; Parastagonospora nodorum
• CAZyme ID: QRC91644.1
• CAZy Family: AA7
• CAZyme Description: Aamy domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A7U2ERF6]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
510		57502.31	4.5378

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PnodorumSN15	17580	321614	132	17448

• Gene Location: location=CP069024:60015-61651(+)

Full Sequence      

MGSEEQKPTPENNTLLQGYEWNCPSDNKHYKRLAAEVPKLKAIGINNIWLPPGCKAANPK
GVGFDIYDLYDLGEFDQKGTRATKWGSKEDLLELSKIAKENGVGLYWDAVLNHKAGADKT
EKCRVVEVDNEDRTKEVGEPYEIEGWLGFDFAGRGDKYSSMKYHWEHFSGTDYNQANEKK
AIYKIVGDNKGWSNSVDNEGGNADYMMFADIDYRHPEVQEDVKNWGVWITKELGLKGFRL
DAVQHFSERFTNEWIENVREQCGKDIFMVGEFWSGDRTVMIDWLADLDHKFSLYDSPLLN
NFARLSTTPDADLRTVFDGSLVQAEPVNAVTVVTNHDTQPGQTMETKIEGFFVPLAYSLI
LLRKEGYPCPFYGDLYGLNEPHETPASCGGKLADLILARKLYAYGDQEDYWNDPNLIGFV
RRGTWDKPAGLACLMSNKGPGEIKMAVGEMHAGEKWTDVLGWEEGEVEIDQDGYGLFKCP
GTSVAIWVKADAQGRDQFPVNFDADIYGKA

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	39	377	8.4e-139	0.9941520467836257

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200457	AmyAc_bac_fung_AmyA	0.0	12	401	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.
236518	PRK09441	0.0	10	488	1	479	cytoplasmic alpha-amylase; Reviewed
200453	AmyAc_arch_bac_plant_AmyA	4.83e-43	15	403	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	2.71e-17	15	342	505	786	alpha-amylase
177990	PLN02361	2.00e-16	15	377	14	326	alpha-amylase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC91644.1|GH13_5	0.0	1	510	1	510
CAE7030307.1|GH13_5	0.0	3	509	20	526
CBX99625.1|GH13_5	0.0	1	509	1	509
SMR46955.1|GH13_5	2.16e-281	10	507	2	499
SMQ47168.1|GH13_5	6.19e-281	10	507	2	499

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1WP6_A	3.22e-151	12	488	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	2.59e-150	12	489	6	484	Alkaline alpha-amylase AmyK from Bacillus sp. KSM-1378 [Bacillus sp. (in: Bacteria)]
1W9X_A	7.36e-149	12	489	2	480	Chain A, Alpha Amylase [Sutcliffiella halmapala]
2GJP_A	8.40e-149	12	489	6	484	Chain A, alpha-amylase [Sutcliffiella halmapala],2GJR_A Chain A, alpha-amylase [Sutcliffiella halmapala]
4UZU_A	1.36e-146	10	488	3	479	Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P19571|AMT6_BACS7	4.91e-150	12	488	39	516	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P06279|AMY_GEOSE	3.16e-145	2	488	29	515	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P06278|AMY_BACLI	6.43e-141	12	489	33	511	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P00692|AMY_BACAM	5.50e-140	7	489	28	513	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P26613|AMY2_SALTY	1.46e-126	12	491	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
0.999736	0.000305

TMHMM  Annotations     

There is no transmembrane helices in QRC91644.1.