CAZyme Information: KIW06534.1

Basic Information

• Species: Verruconis gallopava
• Lineage: Ascomycota; Dothideomycetes; ; Sympoventuriaceae; Verruconis; Verruconis gallopava
• CAZyme ID: KIW06534.1
• CAZy Family: GT1
• CAZyme Description: Aamy domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0D2B5Q4]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
639	KN847535|CGC3	71761.58	5.2027

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_VgallopavaCBS43764	9871	N/A	53	9818

• Gene Location: location=KN847535:903046-905085(-)

Full Sequence      

MGSTSDLPTSAQSVWDPEIQNVINNARTPFHPSPLAWEDQLLYFLLPDRFSNNLENGYKD
NDGNVVDTGSIEAFRPSDANNAVAPNKDPTDWQSHGNVWCGGTIVGLTSKLGYLKRMGIT
AIWIGPVFKQVKTDLNSYHGYGVQDFLDVDPRFGPREEYKSLVQKAHDMGLYVIQDIICN
HSGDVFCYEGDPNPSWKWDDSLQRAVVYPVKGFYDADHRPDTTLPFRKVDASRFPDAAIW
PAEFQDGEAIFTREGKINNWDRDPEYLDGDFYNLKDFRLGASSPDQFVATPALKTLVECY
KYWIAFADLDAFRLDTVKHMGWGPTRYFCNAIHEYAMSIGKNNFMIVGEITGGNESKYDT
VTQTGLNAALGITDLQQALWNLPKGNWSPQAYFDQFRNATYLRQGSHAWLRDKLVTMIDD
HDQVWRGDFKGRFCSDAIGSKMIFPAIALNMTTLGIACIYYGSEQSFDGSGGSGLPGHGA
DQWIRECMFGGKFGAFRSQDRHFFDELGVVYGKISRLAELRRKNLVLTRGRQYLREISGD
GVGFGLPEKFPGGRMESIVAWSRIFNNVEILCAINTDTNGDRTAWVTVDAELNAAGDELV
AIFEERPGQNATALRVEKRANRSVVQLTMPPASFAMFKK

Enzyme Prediction     

No EC number prediction in KIW06534.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	101	470	1.4e-46	0.9364548494983278

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200489	AmyAc_5	0.0	42	520	2	443	Alpha amylase catalytic domain found in an uncharacterized protein 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; 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	5.54e-51	38	524	1	344	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.
200459	AmyAc_AmyMalt_CGTase_like	3.47e-45	38	522	3	388	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.
200479	AmyAc_bac_CMD_like_3	2.14e-35	42	498	6	380	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.
395077	Alpha-amylase	1.28e-33	102	469	1	330	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
QDS72458.1|GH13	4.12e-264	12	638	18	633
ANA39722.1|GH13	2.56e-223	9	639	2	612
QVW34459.1|GH13	9.31e-222	9	639	2	616
ADI85387.1|GH13	9.31e-222	9	639	2	616
AAR36008.1|GH13	9.31e-222	9	639	2	616

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6WNI_A	3.17e-33	36	637	30	518	Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]
5A2A_A	3.67e-31	36	599	5	418	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	6.20e-31	36	599	39	452	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
4E2O_A	4.48e-29	36	469	6	333	Crystal structure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
1QHO_A	5.51e-29	63	638	8	491	FIVE-DOMAIN ALPHA-AMYLASE FROM BACILLUS STEAROTHERMOPHILUS, MALTOSE/ACARBOSE COMPLEX [Geobacillus stearothermophilus],1QHP_A Five-Domain Alpha-Amylase From Bacillus Stearothermophilus, Maltose Complex [Geobacillus stearothermophilus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q05884|AMY_STRLI	1.76e-41	88	543	88	541	Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
sp|P19531|AMYM_GEOSE	3.13e-28	63	638	41	524	Maltogenic alpha-amylase OS=Geobacillus stearothermophilus OX=1422 GN=amyM PE=1 SV=2
sp|P21543|AMYB_PAEPO	4.72e-25	37	469	744	1078	Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
sp|P08704|CDGT_KLEOX	1.78e-24	35	530	38	472	Cyclomaltodextrin glucanotransferase OS=Klebsiella oxytoca OX=571 GN=cgt PE=3 SV=1
sp|P09121|CDGT_BACS3	8.12e-23	28	579	23	466	Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000069	0.000000

TMHMM  Annotations     

There is no transmembrane helices in KIW06534.1.