CAZyme Information: KDQ32476.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ32476.1
• CAZy Family: GT15
• CAZyme Description: glycoside hydrolase family 13 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
466		50942.02	7.2540

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PostreatusPC15	12460	1137138	164	12296

• Gene Location: location=KL198004:42172-44215(+)

Full Sequence      

MAIAITILYLLAAIALNRVGATPLANAPTDSEPTKPDLSSVDKKVIIQLFQWNWKSVAEE
CEHFIGPAGYGYVQVSPPNEHITGNEWWKDYQPVSYKIESRRGNREQFRQMVTKCHAAGV
KVITDTLFNHMSSLSSGKGTGGSTFDKYNYPGLYSYQDFHHKCGSSDEVIHDFRSRKEVQ
TCELLGLADLATGNENAQRRLKAYANDLRSLGVDGFRLDAAKHIPADDLKSILSSVPGFG
TPSFYVTQEVVGGTKDDDSEVKATEYIQNGDVQVFEYSKKIREAFMKGSFTILKDLGRDW
VPSAHANVFVVNHDKERDGEALNANAPSNIYILAHIFSLAYPYGRVSVLSSYEGGLGDKD
VGGPNQGNAKCSGSARNGNGGWMCQHRWVAIAGMTRFRNAVQDAPLENLQSPRDDRIAFS
RGKSGFVAINNSDNPWSATLNTGLPKGSYCDVVSGGAKASKCTGPT

Enzyme Prediction     

No EC number prediction in KDQ32476.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	69	342	7.9e-93	0.9962825278810409

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200456	AmyAc_bac_euk_AmyA	1.19e-138	43	401	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	3.55e-52	45	405	3	349	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	3.38e-27	45	151	2	108	Alpha-amylase domain.
200459	AmyAc_AmyMalt_CGTase_like	1.89e-24	69	327	60	326	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.
214749	Aamy_C	1.34e-14	414	466	8	55	Aamy_C domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAX51638.1|GH13_32	2.32e-162	26	464	6	435
QRV93129.1|CBM20|GH13_32	1.56e-158	31	464	29	451
QRV93130.1|GH13_32	1.61e-157	33	464	31	446
QRV78355.1|GH13_32	1.05e-155	18	464	17	446
QRW03447.1|CBM20|GH13_32	2.31e-155	19	464	10	440

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1G94_A	7.60e-115	47	464	6	418	CRYSTAL STRUCTURE ANALYSIS OF THE TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA AMYLASE FROM PSEUDOALTEROMONAS HALOPLANCTIS IN COMPLEX WITH A HEPTA-SACCHARIDE AND A TRIS MOLECULE [Pseudoalteromonas haloplanktis],1G9H_A TERNARY COMPLEX BETWEEN PSYCHROPHILIC ALPHA-AMYLASE, COMII (PSEUDO TRI-SACCHARIDE FROM BAYER) AND TRIS (2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL) [Pseudoalteromonas haloplanktis],1L0P_A Crystal Structure Analysis Of The Complex Between Psychrophilic Alpha Amylase From Pseudoalteromonas Haloplanctis And Nitrate [Pseudoalteromonas haloplanktis]
1AQH_A	8.89e-115	47	464	6	418	ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis],1AQM_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS [Pseudoalteromonas haloplanktis],1B0I_A ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS [Pseudoalteromonas haloplanktis]
1JD9_A	8.89e-115	47	464	6	418	Chain A, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1JD7_A	1.26e-114	47	464	6	418	Chain A, ALPHA-AMYLASE [Pseudoalteromonas haloplanktis]
1KXH_A	4.30e-114	47	464	6	418	Chain A, alpha-amylase [Pseudoalteromonas haloplanktis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P27350|AMY_STRTL	3.00e-122	13	454	9	429	Alpha-amylase OS=Streptomyces thermoviolaceus OX=1952 GN=amy PE=3 SV=2
sp|P09794|AMY_STRLM	1.23e-119	8	455	10	429	Alpha-amylase OS=Streptomyces limosus OX=1947 GN=aml PE=3 SV=1
sp|P30270|AMY_STRGR	1.38e-118	8	455	10	429	Alpha-amylase OS=Streptomyces griseus OX=1911 GN=amy PE=3 SV=1
sp|P22998|AMY_STRVL	2.12e-115	26	454	23	428	Alpha-amylase OS=Streptomyces violaceus OX=1936 GN=aml PE=2 SV=1
sp|P29957|AMY_PSEHA	1.49e-112	36	464	19	442	Alpha-amylase OS=Pseudoalteromonas haloplanktis OX=228 GN=amy PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000199	0.999776	CS pos: 21-22. Pr: 0.9753

TMHMM  Annotations     

There is no transmembrane helices in KDQ32476.1.