CAZyme Information: KIW19002.1

Basic Information

• Species: Exophiala spinifera
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala spinifera
• CAZyme ID: KIW19002.1
• CAZy Family: GT2
• CAZyme Description: Aamy domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A0D2A270]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1240	KN847493|CGC7	140407.29	6.1217

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EspiniferaCBS89968	12110	N/A	61	12049

• Gene Location: location=KN847493:2709099-2712932(-)

Full Sequence      

MAGSIPALIFAIIALVSALRYEEDQLLWNLNQRVSATKPTDYWGEWENHTFHPSPANWRF
PFYSLILDRFVDGDPSNDNANGTLFEHSWTSNQFRFGGDVRGVQQSLDYLHGMGIRGIYI
IGSPFINFPWGGDGYGPLDFTLLDHHHGTIADWRKLITAIHERDMYVILDNTLATMGDLI
GFKGYLNSTTPFSWDEYDYEWKGTRRYHDFTPNNSINENCEYPRFWGQDGYPTQQEISQG
QHTCYDSDFDQYGDMPGVGEVPTWQSQLAKFASTQDRLRIWRADVMERVQVMSCMQIAML
DIDGFRMDKAFQTPLDAQVEWANYQRDCARRYGKHNFFITGEGVGEPPFEAVYMGRGKQP
DMYFENITEAQLATNQSSIRNASAYLREFGSSALDSAAFHYPTYGALTRFLGLSGLIGSE
GLDWSYHWRKLLERDDMVNANTGEFDPRHMFGTTNQDVFRWPALTYGLERQSLGFLVTQM
LLPGIPLLLWGEEQAFYILENLATDYVFGRMPMASQRAWQLHGCYQLSQTGYYDQPFNKS
RTGCHDDSVSLDHRDPSSPARNLLKRMYQLRQEYPVLNDGYTLRNLSNLTSEIFLPGSAN
IPSEFGVWSVYRGRTEGVQDFSGVGDHGNQGVWFVYMNENATKVYDFNCSDYVKALTSPF
AAGTRVKNLFYPYDEYTLQASRHTLRIEGSEDYNGCLPQLEFEPWGFKAFVPIREWREPM
PTITRVIPHHDARLLSSVPLGSQDKVQLEIRFSSNMSCDSVTNNLQVQSTTQDGVQAQFD
RSSVSCHSQDTDFPDLNGAVATSWIWRGMLSNVSHGIHTYTVSNVTTADGQRYTNARDRF
MFRVGSLDNAMVFPLSSNYTTNMLQKDNATGALSVKALAAGAELYQYSTNWGNTFSPWRT
YTGKPMEIERHSWKGTKAQRWDGTHVILRYWSEIAGSADHVQHTDLEEHLPRRWPHAFVE
GSWNQWGSDRGIRNRMKQSKADLGLWSFDLAAEWPTQVGVNVWGLNSDGTLDLTAAYGDV
DGDHVLDWLPPNTKSTNVVNMTERPPLPHLGWRLVVNDADFSYNIVPIGSAWSQLVVGLL
LGLVPLITALIGVWAFRKSYYHVHFNTRGETAKTGVIPSLKRSLTLFEGSRSMRSSNSVE
SRRPSHSSLPSVVARAPSVHSDESLTSSNAGLRKKSRALSVAADIGAPLRRKTLIATMEY
EIEDWSIKVKIGGLGVMSSLMGKSLSHQDLIWVVPCIGVT

Enzyme Prediction     

EC	2.4.1.183:18	2.4.1.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	97	494	2.4e-162	0.995

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200462	AmyAc_AGS	0.0	8	574	4	569	Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase). Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. 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	1.45e-27	62	594	3	466	Glycosidase [Carbohydrate transport and metabolism].
200478	AmyAc_bac_CMD_like_2	3.84e-22	62	179	5	127	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.
200489	AmyAc_5	2.32e-21	62	386	2	345	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.
200459	AmyAc_AmyMalt_CGTase_like	1.37e-19	63	515	8	369	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
QDS69075.1|GH13_22|GT5	0.0	9	1238	6	1204
AYG85496.1|GH13_22|GT5	0.0	18	1238	25	1215
QZK27799.1|GH13_22|GT5	0.0	18	1238	25	1198
QZK27800.1|GH13_22|GT5	0.0	18	1238	25	1212
BCS01745.1|GH13_22|GT5	0.0	15	1238	20	1220

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4E2O_A	5.24e-14	63	495	13	330	Crystal structure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
6WNI_A	6.00e-12	63	170	37	155	Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNI_B Chain B, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus],6WNU_A Chain A, Cyclomaltodextrin glucanotransferase [Caldanaerobacter subterraneus]
5A2A_A	8.23e-12	63	495	12	329	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	9.48e-12	63	495	46	363	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]
6SAO_A	9.67e-11	56	182	4	126	Structural and functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q09854|MOK11_SCHPO	3.86e-312	28	1238	32	1193	Cell wall alpha-1,3-glucan synthase mok11 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok11 PE=3 SV=2
sp|Q9USK8|AGS1_SCHPO	2.39e-302	16	1238	24	1191	Cell wall alpha-1,3-glucan synthase ags1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ags1 PE=1 SV=3
sp|Q9Y719|MOK13_SCHPO	1.67e-301	8	1238	11	1186	Cell wall alpha-1,3-glucan synthase mok13 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok13 PE=3 SV=2
sp|Q9UUL4|MOK12_SCHPO	2.33e-272	4	1237	5	1216	Cell wall alpha-1,3-glucan synthase mok12 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok12 PE=3 SV=1
sp|Q9Y704|MOK14_SCHPO	2.74e-14	1005	1238	108	302	Cell wall alpha-1,3-glucan synthase mok14 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok14 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.054885	0.945098	CS pos: 18-19. Pr: 0.9052

TMHMM  Annotations     

Start	End
1074	1096