CAZyme Information: SPBC16A3.13.1-p1

Basic Information

• Species: Schizosaccharomyces pombe
• Lineage: Ascomycota; Schizosaccharomycetes; ; Schizosaccharomycetaceae; Schizosaccharomyces; Schizosaccharomyces pombe
• CAZyme ID: SPBC16A3.13.1-p1
• CAZy Family: GT20
• CAZyme Description: alpha-amylase homolog Aah4

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
774	Spom972h_chrII|CGC5	89459.44	7.4848

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Spombe972h	6995	284812	1857	5138

• Gene Location: location=Spom972h_chrII:4272341-4274665(-)

Full Sequence      

MKLSLKDLALSIILVLGVAPPVQALSAEEWKKQSVYNVMTDRFATSKVVPHCDVKAEKYC
GGNWQGIVDHLDYIRDLGFTAISISPVVEQLEGPEYHGEAYHGHRPKNYYRLNPHFGNEE
DLKELSDALHGKGMYLMVDVAINHTISEYFEDDYFKNTYFDKTHIDHKCKEHCSCHHDKF
PRPVPHNGTKPDHKPWKHEEHCHHGKFPRPVPHNGTKPDHKPWKHEEHCSCHHDKFPRPV
PHNGTKPDHKPWKHEEHCSCHHDKFPRPVPHNGTKPDHKPWKHEEHCHHGKFPRPIPHNG
TKPDHKPWKHEEHCHHGRFPRPVPHNGTKPDHKPWKHEEHCSCHHDKFSRPVPHNGTKPD
HKPWKHEEHCHHGKFLRPVPHNVTKPDHKPWKHEEHCHHGKFPRPVPHNGTKPDHKPWKH
EEHCSCHEDHSVHERPSAKGALEDYIQTFVETFQIDGIRFDAMGDKYRKYWPDFCKAAGV
FCMGDLKSSDSLKVCDWQNDLEGLSNFPVRESAVKAFLMNNPEGIVDLADKMTDMRGLCV
NPLLLGNFVENKDLPRMASISSDPATLKNAIAFVLMGDGIPMMYNGQELAMRGEEVPYNR
PAIWEKGFPKRNPYYKFTSTINRFRKAMIESKDGEAFLNMQSDISIVDKRILLLRRGKVI
TVLNNLGSYYIHFHYTVSAEEHKWMDVLSCKSVPVQDNRQVFMVRNGEPMILYPEESAYE
MGLCPSPIQLTEDYNSEGSLSINVEEAQTSKAPEQNRGFTNVLAALLLSLLMIL

Enzyme Prediction     

EC	3.2.1.1:7	3.2.1.1:16

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	284	599	2.9e-74	0.6993464052287581
GH13	61	279	3.6e-56	0.4542483660130719

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200458	AmyAc_euk_AmyA	3.31e-68	434	631	179	375	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.
200458	AmyAc_euk_AmyA	6.74e-63	25	144	1	122	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.
223443	AmyA	3.59e-38	33	415	1	309	Glycosidase [Carbohydrate transport and metabolism].
214758	Aamy	8.45e-31	38	145	2	95	Alpha-amylase domain.
200459	AmyAc_AmyMalt_CGTase_like	1.63e-30	35	145	7	129	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
CAA16864.1|GH13_1	0.0	1	774	1	774
NP_596776.1|GH13_1	0.0	1	774	1	774
BAB60884.1|GH13	2.12e-172	525	774	1	250
CAD62442.2|GH13_1|3.2.1.1	1.79e-75	10	732	11	496
BAB60880.1|GH13_1|3.2.1.1	4.00e-59	434	732	9	306

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VM7_A	1.98e-53	17	724	14	490	Chain A, Alpha-amylase [Malbranchea cinnamomea]
6XSJ_A	2.46e-45	16	726	13	498	Chain A, Alpha-amylase [Aspergillus oryzae],6XSJ_B Chain B, Alpha-amylase [Aspergillus oryzae],6XSV_A Chain A, Alpha-amylase [Aspergillus oryzae]
6YQ7_A	2.46e-45	16	726	13	498	Taka-amylase [Aspergillus oryzae],6YQ7_B Taka-amylase [Aspergillus oryzae],6YQ9_AAA Chain AAA, Alpha-amylase [Aspergillus oryzae],6YQ9_BBB Chain BBB, Alpha-amylase [Aspergillus oryzae],6YQA_AAA Chain AAA, Alpha-amylase [Aspergillus oryzae],6YQA_BBB Chain BBB, Alpha-amylase [Aspergillus oryzae],6YQB_AAA Chain AAA, Alpha-amylase [Aspergillus oryzae],6YQB_BBB Chain BBB, Alpha-amylase [Aspergillus oryzae],6YQC_AAA Chain AAA, Alpha-amylase [Aspergillus oryzae],6YQC_BBB Chain BBB, Alpha-amylase [Aspergillus oryzae]
2TAA_A	3.11e-45	29	724	5	474	Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae],2TAA_B Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae],2TAA_C Structure And Possible Catalytic Residues Of Taka-amylase A [Aspergillus oryzae]
2GUY_A	1.73e-43	29	726	5	477	Orthorhombic crystal structure (space group P21212) of Aspergillus niger alpha-amylase at 1.6 A resolution [Aspergillus oryzae],2GVY_A Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution [Aspergillus oryzae],2GVY_B Monoclinic crystal form of Aspergillus niger alpha-amylase in complex with maltose at 1.8 A resolution [Aspergillus oryzae],3KWX_A Chemically modified Taka alpha-amylase [Aspergillus oryzae],3VX0_A Crystal Structure of alpha-amylase from Aspergillus oryzae [Aspergillus oryzae RIB40],3VX1_A Crystal Structure of alpha-Amylase from Aspergillus oryzae [Aspergillus oryzae RIB40],6TAA_A Structure And Molecular Model Refinement Of Aspergillus Oryzae (Taka) Alpha-Amylase: An Application Of The Simulated-Annealing Method [Aspergillus oryzae],7TAA_A Family 13 Alpha Amylase In Complex With Acarbose [Aspergillus oryzae]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O42918|AMY4_SCHPO	0.0	1	774	1	774	Alpha-amylase 4 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=meu7 PE=1 SV=1
sp|O14154|MDE5_SCHPO	3.19e-76	10	732	11	496	Alpha-amylase mde5 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mde5 PE=2 SV=1
sp|P21567|AMY1_SACFI	6.51e-51	26	721	29	492	Alpha-amylase OS=Saccharomycopsis fibuligera OX=4944 GN=ALP1 PE=3 SV=1
sp|Q02906|AMYB_ASPAW	2.07e-48	16	726	13	498	Alpha-amylase B OS=Aspergillus awamori OX=105351 GN=amyB PE=3 SV=1
sp|Q02905|AMYA_ASPAW	5.19e-48	16	724	13	496	Alpha-amylase A OS=Aspergillus awamori OX=105351 GN=amyA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000230	0.999746	CS pos: 24-25. Pr: 0.9782

TMHMM  Annotations     

There is no transmembrane helices in SPBC16A3.13.1-p1.