CAZyme Information: ACLA_042430-t26_1-p1

Basic Information

• Species: Aspergillus clavatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
• CAZyme ID: ACLA_042430-t26_1-p1
• CAZy Family: GH16
• CAZyme Description: alpha-1,3-glucan synthase Ags3

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2398		269824.37	6.5261

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AclavatusNRRL1	9428	344612	287	9141

• Gene Location: location=DS027056:2670284-2677642(-)

Full Sequence      

MQRLATLLLSLLLSVHQVLCWPYTESLVDYNLNENKSAESPIDYWGEWPDHKYHPSPKNW
RFPVYTIFLDRIANGDPTNDDINGTAFEHVVNSNQMRHGGDLVGLIDSLDYIRGMGFKGI
YFAGTGLMNLPWAYDGYSPVDTTLLDMHHGTLQDWRRTISEIHDRDMYVILDNTLATLSN
LIGFQGHLNDSADFRPDEYHVEWISDRRYADFHFSNEYNESCAYPKFWYETGFPLGSGGV
EKLHGCYNSDFDQYGELEAFGNFPDWQRQLTKFASVQDRLREWHKPVRDIITKHYCIQIA
SLDIDGFRYDKAAQATLEPLGEISAAFRECATKLGKDNFFISGEITSGDTFGSLYLGRGR
QPNQRLNSTIDALKLNNNSAPQYFLREDGHQALDSAAFHYTIYRSMTRFLGMDGNLVAGF
DLNTDFIQAWNEMLVNNDFLNHFTNEVDPRHMYGVSNQDNFRWPAIKNGTAKYLLGLFIV
TLELPGIPLILWGEEQDMYVFDATATNYLFGRQPMTYQTAWWTHGCFNLNTTKFYDFPNE
RGLYGCHDITVTYDQRNPAHPLRNIMKRMFEIREQYPVANDGIYLQTLSQLTKDIYLPGS
STTPTVTGLWSVLRSYFPGIQKEADSKDNSTFWLVYHNDNRTVSYGGDCKKKDTALLAPY
KAGTKLTNLFYPYDELTLQEGPGPIGGPGSESYGCTSNLTLQAWEYRAYVRTEEFVEPGP
TVTEFAPGHDARLLSSEDTGETVDIRLGYSKEMSCDGVTRAISLNSTSQKGITPTLDTSS
VNCTKITPRTSGNGYAGEIPTVWTWSAKLKNVHHGVHEIIVKNVTTTSGLSTNAVDRFLL
RMGSLTNPLMTPLANYSSSLVHKSQDGSIYIQHDAAGADQFRYSTTFGRTWSDWTAYEGG
NTTIDVAPWSGTDAQHWKGTHVRVQYFSRLTGSSDYIQEGDEGWEDDVPRRFPQLWWNGP
YNQYGYDAGLESSMRYDSKERVWKYDFVYEWPSVGQISVWGVGPDGIPDPTEVYGDVANS
SVVQKLPPSYLSSNVINITTLPPFPHLGWTISLNDANLRYVMTPVGSGWAQLVLFVLLWV
VPILMGLFGAFIFMRKFYRVKLNRDGAAAKEVKLPMIWRKIRGHFANKDEAEIDLPDKGI
IANATIAGAPEQRRTVLIATMEYNIEDWNVKVKIGGLGVMAQLMAQNLKHQNLIWAVPCV
GDIEYPEDTPAEPMVVTILDKPYLVNVQYHVVDNITYVILDAPVFRQQTKAEPYPPRMDD
LDSAIYYSAWNQCIAETIKRFPSIDLYHINDFHGCLAPLYLLPTRTIPVCLSLHNAEFQG
LWPLRTQQEKKEVCSVFNLPVETATKYCQFGNVFNLLHTGASYLRFHQHSFGAVGVSKKY
GKRSWARYPIFWSLDKIGSLPNPDPSDTGAVGHGTDATVPIPSPQERINDKLKAQKWAGL
KEDADANLLVFVGRWSKQKGVDLIADVIPAILSSRPEVQLICVGPIIDLYGKLAAVKLEK
IMAMFPGRVFSKPEFTILPPYVFSGADFALIPSRDEPFGLIAVEFGRKGALGIGSRIGGL
GQMPGWWYTVESDATRHLLHQLRTAIKSALDSDLETREEMRTNSAQQRFPVLEWIQKLET
LQRTAIKIHHEKNKDTASGPMPDSQIYWETQNMRDSTVSLPGLPPSLRDGTDSPPARLSL
NAQSRLRELQADDQNSGRLGRKLSLGRRAGPGQGRSRLMKKSLRSSQVAEGQTDDETTDA
DLDEDDLDARLVNYISSEEAMRAVGHDLGSPDIRDSYRSENLGTPSQSMSTSPYYVSRAP
SPAPRAPSELFQHPFQLALHSGASTPSIHSRNVSVLSLPSVKGDHNQQVFELNKVDPTFT
DSMGHFTRRFEEILEGLDKKNSMTDCCIETFLMKSERKFFNMYNDAQLKKHRAKNAVYPS
GAADYVEDETSYNRLSDPGAGTDISDSDEIDRWLSRLGYMRPMAIQRFMRRRVGNWPVYA
LFLGLGQIIATNSAQITLLVGQVGESATKLYVIAAIYCVASIVWWLMYSRLPAVIVLSVP
WFIYGFAFIIIGVSPYGASVASRGWAQNVAAAVYAVASSSGSLFFALNFGDQGSVPVKDW
MFRAGLIQGISQLYTVALWYWSSRVTTVEIGGVSSLTLGTWRLTAVVMPIAAVCFVIGVL
LALGLPNYYRQAPSRILFFYTSLFRRRIVLWFFFMVIVQNWFLAAAFGRNWSFLWSSNHA
KTWQIVVLIICFFLVLWVIILSAFRILSKEHSWILPVFGLSLGAPRWAQTWWGTSNIGYY
LPWAGSLTSGAVVSRSLWLWLGVLDEVQQVGLGMILLQTLTRVHVCFVLLAAQAVGSIAT
ICARGFAPNRLGPDGVSPNVGTSVDKVGNAWFWISLFFQLLASFGFLLFYRKEQLNRP

Enzyme Prediction     

EC	2.4.1.183:18	2.4.1.-:2	2.4.1.183:36	2.4.1.-:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	99	496	1.4e-176	0.995
GH13	1156	1618	1.8e-67	0.9825

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200462	AmyAc_AGS	0.0	16	576	10	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.
340822	GT5_Glycogen_synthase_DULL1-like	2.26e-99	1156	1609	2	459	Glycogen synthase GlgA and similar proteins. This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
223443	AmyA	4.98e-30	64	596	3	466	Glycosidase [Carbohydrate transport and metabolism].
223374	GlgA	3.50e-23	1221	1560	68	403	Glycogen synthase [Carbohydrate transport and metabolism].
200489	AmyAc_5	3.68e-22	65	496	3	395	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
EAL90874.1|GH13_22|GT5|2.4.1.183	0.0	2	2398	6	2412
QMW36665.1|GH13_22|GT5	0.0	1	2398	6	2404
QRD92273.1|GH13_22|GT5	0.0	1	2398	6	2404
BAE66017.1|GH13_22|GT5	0.0	1	2398	6	2404
QMW48721.1|GH13_22|GT5	0.0	1	2398	6	2404

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	2.95e-15	64	172	11	112	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	3.69e-15	64	172	45	146	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	3.55e-13	64	172	12	113	Crystal structure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
3EDF_A	1.67e-12	64	234	109	279	Chain A, Cyclomaltodextrinase [Flavobacterium sp. 92],3EDF_B Chain B, Cyclomaltodextrinase [Flavobacterium sp. 92],3EDJ_A Chain A, Cyclomaltodextrinase [Flavobacterium sp. 92],3EDJ_B Chain B, Cyclomaltodextrinase [Flavobacterium sp. 92],3EDK_A Chain A, Cyclomaltodextrinase [Flavobacterium sp. 92],3EDK_B Chain B, Cyclomaltodextrinase [Flavobacterium sp. 92]
3EDD_A	1.67e-12	64	234	109	279	Chain A, Cyclomaltodextrinase [Flavobacterium sp. 92],3EDD_B Chain B, Cyclomaltodextrinase [Flavobacterium sp. 92]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9UUL4|MOK12_SCHPO	0.0	6	2395	8	2350	Cell wall alpha-1,3-glucan synthase mok12 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok12 PE=3 SV=1
sp|Q09854|MOK11_SCHPO	0.0	20	2398	22	2397	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	0.0	3	2398	10	2410	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	0.0	7	2398	7	2358	Cell wall alpha-1,3-glucan synthase mok13 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok13 PE=3 SV=2
sp|Q9Y704|MOK14_SCHPO	1.39e-279	1020	2398	126	1369	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
0.000295	0.999696	CS pos: 20-21. Pr: 0.9809

TMHMM  Annotations     

Start	End
1072	1094
1973	1990
2010	2028
2033	2055
2065	2087
2100	2122
2145	2167
2188	2207
2222	2244
2325	2347
2367	2389