CAZyme Information: CKF44_05264-t42_1-p1

Basic Information

• Species: Cryptococcus neoformans
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus neoformans
• CAZyme ID: CKF44_05264-t42_1-p1
• CAZy Family: GH72|CBM43
• CAZyme Description: alpha-amylase AmyA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
474		49820.21	4.3703

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CneoformansKN99	6967	N/A	0	6967

• Gene Location: location=CP022324.1:881110-882748(+)

Full Sequence      

MYLMVDIAINALAATSYSLDASALASDADGTLLFKDPSDFHTRCDISWGNHTSEQVCWLV
TGDDDGGVALLDLKTESDSVASVLKDWVGGYVTEYRIDGFRIDASKHMSKKFQHDFCQAA
GTFCMGEVAGDNTEYAGEYQGADGIDSVCGFGLMYGFVNVFTAGDKMSTLEYYINLAASS
YPDPTVIGTFLDNQDLPRFNSLTSDASLVYNAIVGLFMYGGVPIVYYGLEQDISDGPTDP
QNREALWNYNSYATDGVTFGRITNLNKIRKRLGGVGKLYKTVATVLATQDQDIALQREEV
LTVLTNRGTSGSGTWAIKGTKFGNSASVIDLLSCSTSTTDSNGSLTVTWTSGEPFVFVSS
SVADQAGLCGSLPNGTNAITASSSSVSISIVPVTSSASTNGNLAAITEGSSTPSSFSVSS
ALSSNTSWYTATSAASSVSSSGSVVVVAAVSTASVAVSSSGSICRRSKKSRRQL

Enzyme Prediction     

No EC number prediction in CKF44_05264-t42_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	1	242	5.4e-67	0.7581699346405228

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200458	AmyAc_euk_AmyA	8.19e-108	1	274	112	374	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.
200478	AmyAc_bac_CMD_like_2	2.10e-34	72	270	126	342	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
370390	DUF1966	4.41e-25	285	369	1	90	Domain of unknown function (DUF1966). This domain is found in various fungal alpha-amylase proteins. Its exact function has not, as yet, been defined.
395077	Alpha-amylase	3.53e-20	72	240	142	334	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.
200451	AmyAc_family	1.30e-19	87	227	101	253	Alpha amylase catalytic domain family. 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; and 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 this 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
AGV14255.1|GH13_1	1.21e-317	1	474	1	474
AUB24185.1|GH13_1	1.21e-317	1	474	1	474
AFR94522.1|GH13_1	1.46e-315	1	474	129	602
AUB24184.1|GH13_1	1.46e-315	1	474	129	602
UOH84714.1|GH13_1	1.88e-283	1	474	129	602

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3VM7_A	1.11e-57	1	369	132	490	Chain A, Alpha-amylase [Malbranchea cinnamomea]
2TAA_A	9.65e-50	1	356	112	461	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]
6SAO_A	6.14e-49	1	361	104	439	Structural and functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
6SAV_B	1.18e-46	1	359	104	437	Structural and functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Rhizomucor pusillus]
6SAV_A	1.64e-46	1	359	104	437	Structural and functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Rhizomucor pusillus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P21567|AMY1_SACFI	1.25e-53	1	365	139	491	Alpha-amylase OS=Saccharomycopsis fibuligera OX=4944 GN=ALP1 PE=3 SV=1
sp|Q08806|AMY2_SCHOC	3.18e-52	1	369	144	505	Alpha-amylase 2 OS=Schwanniomyces occidentalis OX=27300 GN=SWA2 PE=3 SV=1
sp|P19269|AMY1_SCHOC	1.31e-49	1	369	148	510	Alpha-amylase 1 OS=Schwanniomyces occidentalis OX=27300 GN=AMY1 PE=1 SV=1
sp|Q02906|AMYB_ASPAW	1.97e-47	1	371	133	498	Alpha-amylase B OS=Aspergillus awamori OX=105351 GN=amyB PE=3 SV=1
sp|Q02905|AMYA_ASPAW	2.69e-47	1	356	133	483	Alpha-amylase A OS=Aspergillus awamori OX=105351 GN=amyA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.986823	0.013177

TMHMM  Annotations     

There is no transmembrane helices in CKF44_05264-t42_1-p1.