dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000000971_01797

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Basic Information help

Species

UMGS1518 sp900552575

Lineage

Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; Victivallaceae; UMGS1518; UMGS1518 sp900552575

CAZyme ID

MGYG000000971_01797

CAZy Family

GH13

CAZyme Description

1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
669		76478.52	6.442

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000971	3501016	MAG	Australia	Oceania

Gene Location

Start: 981; End: 2990 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.18

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	222	512	2.2e-134	0.9965870307167235

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd11321	AmyAc_bac_euk_BE	0.0	154	556	1	406	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.
PLN02447	PLN02447	0.0	44	664	96	727	1,4-alpha-glucan-branching enzyme
PLN02960	PLN02960	8.01e-173	110	666	333	890	alpha-amylase
PLN03244	PLN03244	1.66e-143	110	666	338	865	alpha-amylase; Provisional
COG0296	GlgB	5.09e-96	55	667	26	628	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QSH41972.1	0.0	6	668	9	671
AVM44237.1	0.0	5	667	8	663
ABC76467.1	3.50e-289	14	667	3	660
QBG47429.1	2.00e-283	4	669	2	670
ARN55801.1	1.47e-282	6	667	10	670

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BZY_A	7.45e-204	11	669	32	699	Crystalstructure 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]
5CLT_A	1.26e-201	17	669	6	667	Crystalstructure 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]
7ML5_A	2.67e-190	14	643	16	660	ChainA, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]
3AMK_A	3.91e-190	14	643	17	661	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
3VU2_A	1.11e-189	14	643	17	661	Structureof 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	Description
Q04446	1.44e-203	11	669	32	699	1,4-alpha-glucan-branching enzyme OS=Homo sapiens OX=9606 GN=GBE1 PE=1 SV=3
Q6CCT1	1.14e-202	14	667	9	684	1,4-alpha-glucan-branching enzyme OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=GLC3 PE=3 SV=1
Q6EAS5	1.69e-201	11	669	29	696	1,4-alpha-glucan-branching enzyme OS=Equus caballus OX=9796 GN=GBE1 PE=1 SV=1
P30924	2.26e-201	11	643	99	746	1,4-alpha-glucan-branching enzyme OS=Solanum tuberosum OX=4113 GN=SBE1 PE=2 SV=2
Q555Q9	2.73e-200	14	669	17	678	1,4-alpha-glucan-branching enzyme OS=Dictyostelium discoideum OX=44689 GN=glgB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000039	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000000971_01797.