CAZyme Information: RVD81909.1

Basic Information

• Species: Arthrobotrys flagrans
• Lineage: Ascomycota; Orbiliomycetes; ; Orbiliaceae; Arthrobotrys; Arthrobotrys flagrans
• CAZyme ID: RVD81909.1
• CAZy Family: AA9
• CAZyme Description: Alpha-amylase [Source:UniProtKB/TrEMBL;Acc:A0A436ZSL3]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
788	SAEB01000012|CGC29	85743.30	6.4901

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AflagransCBSH-5679	9927	N/A	30	9897

• Gene Location: location=SAEB01000012:5916821-5919733(+)

Full Sequence      

MKFLGLLKFFIFSLACLFSSVHASVLGRRALPVSLNSYTYANNVLSGSINVQNIAYQKVV
SVYWAQGNNWQSTPIPAVYSSGPVSGYETWVFSGTAVGATELYIKYDVSGTSYYYPGNYV
NVQVTSSTTTTTTTTTTTTSHTTTTLGTTASTTGQTISTLATSTTSAPPFTGTVSPSAIP
SFRVEPVPYEVPATSPSGCGNFNGKDSCSSGSFPDSSENRRWQTPPESDLQYVSSFQSYG
KLVGYADIQYNSARTAAVVVINCLSKTGASLTYYVNNVAQTSNLVQVSTANTGGLNIRIT
DSTGGSLTLETLYFLWENPAISGGLSNFNDGQKGAIVELFGWPYDDVANECAFLSKAGYM
GVKIWPPQEHVWGSNYYETDNQFRPWYFVYQPVSYRLHSRSGTREQLRNMIKSCRSVGVR
VYADAVINHMTANGNDIQNHRNTDCSTYTGHNATDGSPYFTSGNTYLINPYTGTRAAPEY
PSVPYGPSDFHCDCALNSWTDGAIINNCWLVGLVDLNTEKPYVQDRIATYLADLLSIGFS
GFRVDAAKHIGPTSMAQILARFKQKLGGGTLPADWISWHEVIMGGEANLLACSGGEWSWY
TNFNNKLSGVGFSQTDIDKTKIWSSDYPKEHPVCGSWIIPSTRFVIQNDDHDQQNPGSSS
RDMQDKGSVLIKSKDVAAHRAFEVQLFTRTDGNWQIRNILSSYMFMDNGASGYPDGLSDC
SLYTGSQSQSGCLGVPYDQAYVANACGYTMSQGKYTRVHRDLSIINAMRGWVGLGSTTAS
ALGISGCS

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	358	587	8.9e-54	0.6765799256505576

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	1.62e-134	333	774	1	329	Alpha amylase catalytic domain found in bacterial and eukaryotic 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 proteins from bacteria, fungi, mammals, insects, mollusks, and nematodes. 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.
200454	AmyAc_bac1_AmyA	9.74e-36	334	551	2	179	Alpha amylase catalytic domain found in bacterial 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 Firmicutes, Proteobacteria, Actinobacteria, and Cyanobacteria. 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.
214758	Aamy	1.30e-19	344	434	18	99	Alpha-amylase domain.
200458	AmyAc_euk_AmyA	3.15e-15	395	553	88	214	Alpha amylase catalytic domain found in eukaryotic 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 eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
395077	Alpha-amylase	2.76e-10	353	586	27	214	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
EGX42980.1|CBM21|GH13	0.0	20	788	29	790
QRW16798.1|CBM21|GH13	1.08e-255	28	788	27	784
QRV88491.1|CBM21|GH13	3.73e-253	19	788	65	844
QRV73700.1|CBM21|GH13	2.75e-250	14	784	54	839
QRW02641.1|CBM21|GH13	2.75e-250	14	784	54	839

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1VIW_A	2.65e-42	326	716	4	339	TENEBRIO MOLITOR ALPHA-AMYLASE-INHIBITOR COMPLEX [Tenebrio molitor]
1CLV_A	2.65e-42	326	716	4	339	YELLOW MEAL WORM ALPHA-AMYLASE IN COMPLEX WITH THE AMARANTH ALPHA-AMYLASE INHIBITOR [Tenebrio molitor],1JAE_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE [Tenebrio molitor],1TMQ_A STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR [Tenebrio molitor]
1PIF_A	1.02e-41	333	712	10	351	PIG ALPHA-AMYLASE [Sus scrofa],1PIG_A PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE OLIGOSACCHARIDE V-1532 [Sus scrofa],4X0N_A Porcine pancreatic alpha-amylase in complex with helianthamide, a novel proteinaceous inhibitor [Sus scrofa]
3DHP_A	1.88e-41	326	654	4	302	Chain A, Alpha-amylase 1 [Homo sapiens]
1PPI_A	2.55e-41	333	712	10	351	THE ACTIVE CENTER OF A MAMMALIAN ALPHA-AMYLASE. THE STRUCTURE OF THE COMPLEX OF A PANCREATIC ALPHA-AMYLASE WITH A CARBOHYDRATE INHIBITOR REFINED TO 2.2 ANGSTROMS RESOLUTION [Sus scrofa]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P81641|AMYB_DROME	8.97e-47	326	587	22	249	Alpha-amylase B OS=Drosophila melanogaster OX=7227 GN=Amy-d PE=3 SV=3
sp|P08144|AMYA_DROME	8.97e-47	326	587	22	249	Alpha-amylase A OS=Drosophila melanogaster OX=7227 GN=Amy-p PE=2 SV=1
sp|P54215|AMYA_DROMA	8.97e-47	326	587	22	249	Alpha-amylase A OS=Drosophila mauritiana OX=7226 GN=Amy-d PE=3 SV=1
sp|O97396|AMY_PHACE	2.62e-46	309	660	3	313	Alpha-amylase OS=Phaedon cochleariae OX=80249 PE=2 SV=1
sp|Q9BN01|AMYB_DROYA	2.73e-45	326	587	22	249	Alpha-amylase B OS=Drosophila yakuba OX=7245 GN=Amy-d PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000282	0.999677	CS pos: 23-24. Pr: 0.9790

TMHMM  Annotations     

There is no transmembrane helices in RVD81909.1.