CAZyme Information: KLU85608.1

Basic Information

• Species: Magnaporthiopsis poae
• Lineage: Ascomycota; Sordariomycetes; ; Magnaporthaceae; Magnaporthiopsis; Magnaporthiopsis poae
• CAZyme ID: KLU85608.1
• CAZy Family: GH12
• CAZyme Description: alpha-amylase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
456		52473.90	5.3594

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_MpoaeATCC64411	12363	644358	200	12163

• Gene Location: location=GL876968:3454122-3456128(-)

Full Sequence      

MRHVFLTLYPGERYDLGEFDQKGSVATKWGTKEELKRLCSNAKENGVGIYWDAVLNHKFA
ADHKEKCPAAEVDEQDRNKFISDKYEITAWVGFDFPGRNGKYSEQKYHWYHFSGVDFNEA
NGKKAIYKIMGDQNQGWAEDGDVDSEKGNYDYLMGSDLDYSHPEVEKDVLNWGAWLAGEL
PLAGIRFDAVKHYSEDFLRKFISMMDDKYGRGWFFVGEFWKDSLNDMSRYLARMGKKFSL
FDVPLVYNFSQISQGNSADMRKVFDDTLVQREPVNAVTLVMNHDTQPYQALEAPIADWFK
PLAYALILLRTSGYPCVWYGDLYGIKGEHPFPPSCWGALPKLMLARKLYAYGEQADYFDY
QTCLGWVKYGTWDRPHGCAVVLSNAGPGEKRMHVGEMHAGERWTDVLGWSDREVEIGRDG
FGVFRCGQCSVSVYVNKDAKGRERFSEHFDTNIYDE

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	13	325	7e-128	0.9064327485380117

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
236518	PRK09441	0.0	14	435	62	479	cytoplasmic alpha-amylase; Reviewed
200457	AmyAc_bac_fung_AmyA	0.0	14	348	60	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	4.68e-24	10	350	53	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.
223443	AmyA	5.55e-13	30	374	74	414	Glycosidase [Carbohydrate transport and metabolism].
200459	AmyAc_AmyMalt_CGTase_like	1.41e-11	30	321	101	347	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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
QBZ60907.1|GH13_5	9.81e-291	14	456	69	511
QMU23797.1|GH13_5	2.03e-283	14	456	68	509
UQC75400.1|GH13_5	4.50e-276	14	456	406	847
ANH56422.1|GH13_5	2.35e-266	16	454	70	508
CAP70916.1|GH13_5	6.12e-265	14	454	78	520

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VJS_A	4.42e-131	14	437	62	483	Structure Of Alpha-Amylase Precursor [Bacillus licheniformis]
1UD2_A	2.28e-130	14	437	62	480	Crystal structure of calcium-free alpha-amylase from Bacillus sp. strain KSM-K38 (AmyK38) [Bacillus sp. KSM-K38],1UD4_A Crystal structure of calcium free alpha amylase from Bacillus sp. strain KSM-K38 (AmyK38, in calcium containing solution) [Bacillus sp. KSM-K38],1UD5_A Crystal structure of AmyK38 with rubidium ion [Bacillus sp. KSM-K38],1UD6_A Crystal structure of AmyK38 with potassium ion [Bacillus sp. KSM-K38],1UD8_A Crystal structure of AmyK38 with lithium ion [Bacillus sp. KSM-K38]
1UD3_A	2.28e-130	14	437	62	480	Chain A, amylase [Bacillus sp. KSM-K38]
3BH4_A	5.03e-130	10	437	56	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]
6TOY_A	8.08e-129	14	437	62	483	Crystal structure of Bacillus paralicheniformis wild-type alpha-amylase [Bacillus licheniformis],6TOZ_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with acarbose [Bacillus licheniformis],6TP0_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltose [Bacillus licheniformis],6TP1_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with maltotetraose [Bacillus licheniformis],6TP2_A Crystal structure of Bacillus paralicheniformis alpha-amylase in complex with beta-cyclodextrin [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P06278|AMY_BACLI	2.01e-130	14	437	91	512	Alpha-amylase OS=Bacillus licheniformis OX=1402 GN=amyS PE=1 SV=1
sp|P00692|AMY_BACAM	6.88e-129	10	437	87	514	Alpha-amylase OS=Bacillus amyloliquefaciens OX=1390 PE=1 SV=1
sp|P19571|AMT6_BACS7	2.26e-125	14	437	97	518	Glucan 1,4-alpha-maltohexaosidase OS=Bacillus sp. (strain 707) OX=1416 PE=1 SV=1
sp|P06279|AMY_GEOSE	5.33e-117	14	435	97	515	Alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyS PE=1 SV=3
sp|P26613|AMY2_SALTY	7.39e-106	14	438	62	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
1.000027	0.000004

TMHMM  Annotations     

There is no transmembrane helices in KLU85608.1.