dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000004348_00179

You are here: Home > Sequence: MGYG000004348_00179

Basic Information help

Species

Lineage

Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Prevotella;

CAZyme ID

MGYG000004348_00179

CAZy Family

GH13

CAZyme Description

1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
690	MGYG000004348_1\|CGC1	79522.55	6.479

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004348	1551350	MAG	Israel	Asia

Gene Location

Start: 198349; End: 200421 Strand: -

Full Sequence Download help

Enzyme Prediction help

EC	2.4.1.18

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	241	532	6.4e-146	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	8	686	43	727	1,4-alpha-glucan-branching enzyme
cd11321	AmyAc_bac_euk_BE	0.0	172	576	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.
PLN02960	PLN02960	2.70e-152	106	688	303	890	alpha-amylase
PLN03244	PLN03244	5.06e-132	94	688	298	865	alpha-amylase; Provisional
COG0296	GlgB	2.66e-108	62	688	14	627	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
QNT66029.1	23	690	33	699
VEH15409.1	1	690	1	690
QUB46822.1	1	689	21	710
ALO48673.1	23	690	6	672
AGB28031.1	10	690	14	695

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4BZY_A	2.42e-194	27	687	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	2.06e-192	34	687	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	1.18e-183	24	662	10	659	Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
7ML5_A	3.24e-183	24	662	9	658	ChainA, Isoform 2 of 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic [Oryza sativa Japonica Group]
3VU2_A	3.34e-183	24	662	10	659	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
Q555Q9	3.35e-212	20	689	9	676	1,4-alpha-glucan-branching enzyme OS=Dictyostelium discoideum OX=44689 GN=glgB PE=3 SV=1
Q8NKE1	1.74e-205	26	687	15	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
Q96VA4	1.01e-200	20	687	13	683	1,4-alpha-glucan-branching enzyme OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=gbeA PE=2 SV=1
Q6CCT1	8.64e-200	25	686	3	681	1,4-alpha-glucan-branching enzyme OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=GLC3 PE=3 SV=1
Q9Y8H3	2.75e-199	15	687	3	678	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

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
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000004348_00179.