dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: AMAG_00200-t26_1-p1

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Basic Information help

Species

Allomyces macrogynus

Lineage

Blastocladiomycota; Blastocladiomycetes; ; Blastocladiaceae; Allomyces; Allomyces macrogynus

CAZyme ID

AMAG_00200-t26_1-p1

CAZy Family

AA11

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
805		89694.49	6.7604

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AmacrogynusATCC38327	19333	578462	535	18798

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.18:166	2.4.1.18:50

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	283	579	4.2e-150	0.9965870307167235

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200460	AmyAc_bac_euk_BE	0.0	215	621	1	404	Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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.
215246	PLN02447	0.0	65	782	61	730	1,4-alpha-glucan-branching enzyme
215519	PLN02960	6.51e-176	155	782	322	891	alpha-amylase
178782	PLN03244	4.46e-142	163	782	336	866	alpha-amylase; Provisional
223373	GlgB	4.06e-103	126	782	41	628	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
8.54e-289	54	780	16	696
5.48e-285	66	783	28	696
5.48e-285	66	783	28	696
5.48e-285	66	783	28	696
5.48e-285	66	783	28	696

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.56e-270	61	780	26	695	Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_B Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_C Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens]
1.63e-266	73	780	6	663	Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLW_A Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens]
1.81e-230	57	776	4	686	Structure of the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
4.96e-230	57	776	3	685	Chain A, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]
5.13e-230	57	776	4	686	Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group],3VU2_B Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
2.91e-285	64	780	14	680	1,4-alpha-glucan-branching enzyme OS=Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OX=747089 GN=GLC3 PE=2 SV=2
3.47e-279	66	783	12	681	1,4-alpha-glucan-branching enzyme OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=be1 PE=2 SV=3
5.88e-279	61	783	12	686	1,4-alpha-glucan-branching enzyme OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=gbeA PE=2 SV=1
7.77e-272	50	780	12	692	1,4-alpha-glucan-branching enzyme OS=Equus caballus OX=9796 GN=GBE1 PE=1 SV=1
2.82e-270	61	780	26	695	1,4-alpha-glucan-branching enzyme OS=Homo sapiens OX=9606 GN=GBE1 PE=1 SV=3

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000030	0.000000

TMHMM Annotations help

There is no transmembrane helices in AMAG_00200-t26_1-p1.