dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001085_01194

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Basic Information help

Species

RC9 sp000434935

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp000434935

CAZyme ID

MGYG000001085_01194

CAZy Family

GH13

CAZyme Description

1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
657		75686.63	5.829

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001085	2352626	MAG	Sweden	Europe

Gene Location

Start: 138805; End: 140778 Strand: +

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.18

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	218	509	5.8e-143	0.9965870307167235

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PLN02447	PLN02447	0.0	6	652	61	727	1,4-alpha-glucan-branching enzyme
cd11321	AmyAc_bac_euk_BE	0.0	150	552	1	405	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.
PLN02960	PLN02960	1.79e-174	109	656	336	894	alpha-amylase
PLN03244	PLN03244	2.52e-137	109	652	341	863	alpha-amylase; Provisional
COG0296	GlgB	6.61e-103	51	653	26	626	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
ACM90989.1	0.0	7	656	4	665
AZS28218.1	2.94e-289	7	653	5	657
QRO49262.1	2.26e-286	7	653	5	657
ADY31393.1	2.31e-283	11	653	9	657
SNV25929.1	2.31e-283	11	653	9	657

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BZY_A	5.11e-201	7	653	31	695	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	9.89e-198	14	653	6	663	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]
3AMK_A	3.42e-185	4	629	10	650	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
3VU2_A	9.69e-185	4	629	10	650	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]
7ML5_A	1.33e-184	4	629	9	649	ChainA, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [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
Q555Q9	1.16e-206	2	656	8	677	1,4-alpha-glucan-branching enzyme OS=Dictyostelium discoideum OX=44689 GN=glgB PE=3 SV=1
Q6CCT1	2.53e-206	7	652	5	681	1,4-alpha-glucan-branching enzyme OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=GLC3 PE=3 SV=1
Q6EAS5	1.21e-203	7	653	28	692	1,4-alpha-glucan-branching enzyme OS=Equus caballus OX=9796 GN=GBE1 PE=1 SV=1
Q96VA4	1.99e-202	7	653	17	683	1,4-alpha-glucan-branching enzyme OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=gbeA PE=2 SV=1
Q8NKE1	2.31e-202	7	653	16	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

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
1.000049	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001085_01194.