dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: MGYG000001823_00288

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Basic Information help

Species

UMGS1603 sp900553265

Lineage

Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-74; UMGS1603; UMGS1603 sp900553265

CAZyme ID

MGYG000001823_00288

CAZy Family

GH13

CAZyme Description

1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
674	MGYG000001823_3\|CGC1	77376.78	6.8185

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001823	2784400	MAG	Denmark	Europe

Gene Location

Start: 63021; End: 65045 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.18

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	225	516	8.6e-144	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	155	560	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	11	674	61	732	1,4-alpha-glucan-branching enzyme
PLN02960	PLN02960	5.35e-159	111	671	333	890	alpha-amylase
PLN03244	PLN03244	9.40e-135	111	671	338	865	alpha-amylase; Provisional
COG0296	GlgB	5.30e-123	54	672	23	628	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
QUA53617.1	7	673	7	673
AHF24692.1	7	674	7	674
QTE68764.1	9	674	9	674
QUC67824.1	9	674	9	674
QTE71422.1	9	674	9	674

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BZY_A	1.54e-220	11	674	30	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	1.46e-217	18	674	5	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]
3AMK_A	2.63e-208	12	674	13	694	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
7ML5_A	5.11e-208	12	674	12	693	ChainA, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]
3VU2_A	7.47e-208	12	674	13	694	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
Q8NKE1	1.37e-221	12	669	16	679	1,4-alpha-glucan-branching enzyme OS=Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OX=747089 GN=GLC3 PE=2 SV=2
Q6T308	1.53e-219	11	674	27	696	1,4-alpha-glucan-branching enzyme OS=Felis catus OX=9685 GN=GBE1 PE=2 SV=1
Q9D6Y9	1.69e-219	11	674	30	699	1,4-alpha-glucan-branching enzyme OS=Mus musculus OX=10090 GN=Gbe1 PE=1 SV=1
Q04446	1.69e-219	11	674	30	699	1,4-alpha-glucan-branching enzyme OS=Homo sapiens OX=9606 GN=GBE1 PE=1 SV=3
Q6EAS5	4.96e-218	11	674	27	696	1,4-alpha-glucan-branching enzyme OS=Equus caballus OX=9796 GN=GBE1 PE=1 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
1.000077	0.000001	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000001823_00288.