dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Lineage

Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Gemmiger;

CAZyme ID

MGYG000004732_01995

CAZy Family

CBM48

CAZyme Description

1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
570	MGYG000004732_37\|CGC1	63297.66	5.7198

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004732	2775580	MAG	China	Asia

Gene Location

Start: 15076; End: 16788 Strand: +

Enzyme Prediction help

No EC number prediction in MGYG000004732_01995.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	165	443	8.7e-71	0.9966777408637874
CBM48	20	99	1.8e-16	0.868421052631579

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
PRK12313	PRK12313	1.09e-158	8	515	15	557	1,4-alpha-glucan branching protein GlgB.
PRK05402	PRK05402	2.85e-145	14	517	114	655	1,4-alpha-glucan branching protein GlgB.
cd11322	AmyAc_Glg_BE	3.85e-125	105	479	3	402	Alpha amylase catalytic domain found in the Glycogen branching enzyme (also called 1,4-alpha-glucan branching enzyme). The glycogen branching enzyme catalyzes the third step of glycogen biosynthesis by the cleavage of an alpha-(1,4)-glucosidic linkage and the formation a new alpha-(1,6)-branch by subsequent transfer of cleaved oligosaccharide. They are part of a group called branching enzymes which catalyze the formation of alpha-1,6 branch points in either glycogen or starch. This group includes proteins from bacteria, eukaryotes, and archaea. 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.
COG0296	GlgB	4.81e-122	8	569	14	628	1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK12568	PRK12568	2.14e-105	8	523	115	666	glycogen branching enzyme; Provisional

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATO99239.1	9.66e-133	8	570	10	614
QIA42361.1	9.66e-133	8	570	10	614
ATL89501.1	1.36e-132	8	570	10	614
AXB29572.1	1.50e-129	8	570	10	615
CBL00737.1	4.22e-129	8	570	10	615

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6JOY_A	7.56e-109	2	523	6	556	TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
1M7X_A	2.05e-90	11	509	5	539	TheX-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_B The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_C The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_D The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli]
4LPC_A	3.56e-90	28	509	21	534	CrystalStructure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_B Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_C Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_D Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LQ1_A Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_B Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_C Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_D Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],5E6Y_A Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_B Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_C Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_D Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_A Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_B Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_C Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_D Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_A Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_B Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_C Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_D Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A]
3K1D_A	8.51e-90	4	516	105	652	Crystalstructure of glycogen branching enzyme synonym: 1,4-alpha-D-glucan:1,4-alpha-D-GLUCAN 6-glucosyl-transferase from mycobacterium tuberculosis H37RV [Mycobacterium tuberculosis H37Rv]
5GR2_A	1.07e-86	4	521	133	709	Crystalstructure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GR4_A Crystal structure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q93HU3	4.14e-108	2	523	6	556	1,4-alpha-glucan branching enzyme GlgB OS=Rhodothermus marinus OX=29549 GN=glgB PE=1 SV=1
P30537	6.93e-108	8	490	14	520	1,4-alpha-glucan branching enzyme GlgB OS=Bacillus caldolyticus OX=1394 GN=glgB PE=1 SV=1
A1VC54	9.72e-108	4	516	15	566	1,4-alpha-glucan branching enzyme GlgB OS=Desulfovibrio vulgaris subsp. vulgaris (strain DP4) OX=391774 GN=glgB PE=3 SV=1
Q729V5	2.71e-107	4	516	15	566	1,4-alpha-glucan branching enzyme GlgB OS=Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough) OX=882 GN=glgB PE=3 SV=1
P30538	5.69e-106	8	514	14	546	1,4-alpha-glucan branching enzyme GlgB OS=Geobacillus stearothermophilus OX=1422 GN=glgB 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
1.000047	0.000004	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000004732_01995.

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