dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Melampsora larici-populina

Lineage

Basidiomycota; Pucciniomycetes; ; Melampsoraceae; Melampsora; Melampsora larici-populina

CAZyme ID

MELLADRAFT_38296-t26_1-p1

CAZy Family

GH16

CAZyme Description

family 5 glycoside hydrolase family 13/glycosyltransferase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2348	GL883127\|CGC3	263208.42	6.4565

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Mlarici-populina98AG31	16380	747676	8	16372

Gene Location

Enzyme Prediction help

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

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	107	513	6e-146	0.9975
GH13	1165	1631	1.3e-79	0.985

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200462	AmyAc_AGS	0.0	10	592	1	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	9.49e-99	1165	1630	1	464	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.
223374	GlgA	6.03e-26	1911	2318	121	487	Glycogen synthase [Carbohydrate transport and metabolism].
223443	AmyA	6.44e-25	72	618	3	463	Glycosidase [Carbohydrate transport and metabolism].
200478	AmyAc_bac_CMD_like_2	3.05e-24	72	190	5	126	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.

CAZyme Hits help

E-Value	Query Start	Query End	Hit Start
25	2335	23	2348
25	2335	23	2348
25	2335	23	2348
26	2335	22	2415
26	2335	32	2425

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
9.49e-14	1295	1573	131	401	Chain A, Glycogen synthase [Escherichia coli]
9.82e-14	1295	1573	131	401	Crystal Structure of Wild-type E.coli GS in complex with ADP and Glucose(wtGSb) [Escherichia coli],2R4T_A Crystal Structure of Wild-type E.coli GS in Complex with ADP and Glucose(wtGSc) [Escherichia coli],2R4U_A Crystal Structure of Wild-type E.coli GS in complex with ADP and Glucose(wtGSd) [Escherichia coli],3GUH_A Crystal Structure of Wild-type E.coli GS in complex with ADP and DGM [Escherichia coli K-12]
3.08e-13	63	189	23	144	Chain A, Alpha-amylase [Malbranchea cinnamomea]
5.25e-13	1295	1573	131	401	Chain A, Glycogen synthase [Escherichia coli],3CX4_A Chain A, Glycogen synthase [Escherichia coli]
1.65e-11	65	555	4	347	Structural and functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
0.0	23	2335	21	2353	Cell wall alpha-1,3-glucan synthase mok13 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok13 PE=3 SV=2
0.0	25	2335	24	2392	Cell wall alpha-1,3-glucan synthase mok11 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok11 PE=3 SV=2
0.0	17	2335	20	2405	Cell wall alpha-1,3-glucan synthase ags1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ags1 PE=1 SV=3
0.0	11	2335	9	2348	Cell wall alpha-1,3-glucan synthase mok12 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok12 PE=3 SV=1
4.68e-282	1046	2335	148	1364	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 help

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000196	0.999789	CS pos: 23-24. Pr: 0.9805

TMHMM Annotations download full data without filtering help

Start	End
1909	1931
1946	1963
1970	1992
2007	2029
2038	2060
2080	2102
2125	2144
2159	2181
2188	2210
2230	2252
2259	2278
2314	2332
1075	1097

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