dbCAN-seq: a database of CAZyme sequence and annotation

Basic Information help

Species

Stenotrophomonas bentonitica_A

Lineage

Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas bentonitica_A

CAZyme ID

MGYG000002381_03257

CAZy Family

CBM48

CAZyme Description

1,4-alpha-glucan branching enzyme GlgB

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
746	MGYG000002381_59\|CGC1	81664.55	5.8779

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002381	4114425	Isolate	not provided	not provided

Gene Location

Start: 31147; End: 33387 Strand: +

Enzyme Prediction help

EC	2.4.1.18

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH13	293	593	4e-158	0.9966777408637874
CBM48	141	228	2.6e-22	0.9078947368421053

CDD Domains download full data without filtering help

Cdd ID	Domain	qStart	qEnd	sStart	sEnd	Domain Description
PRK12313	PRK12313	142	746	27	629	1,4-alpha-glucan branching protein GlgB.
PRK14706	PRK14706	122	746	7	623	glycogen branching enzyme; Provisional
PRK14705	PRK14705	35	742	511	1220	glycogen branching enzyme; Provisional
cd11322	AmyAc_Glg_BE	232	629	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.
PRK05402	PRK05402	41	746	15	725	1,4-alpha-glucan branching protein GlgB.

CAZyme Hits help

Hit ID	Query Start	Query End	Hit Start	Hit End
AOX60864.1	1	746	1	746
QHB71729.1	22	744	22	744
QNR98962.1	7	746	4	744
AER57535.1	16	745	15	740
QNH15563.1	34	745	32	748

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4LPC_A	1.80e-253	142	746	9	611	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]
1M7X_A	2.15e-253	142	746	14	616	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]
3K1D_A	4.76e-233	33	742	11	719	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]
5GQW_A	3.25e-222	42	745	40	774	Crystalstructure of branching enzyme W610N mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GQX_A Crystal structure of branching enzyme W610N mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]
5GQZ_A	6.51e-222	42	745	40	774	Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]

Swiss-Prot Hits download full data without filtering help

Hit ID	Query Start	Query End	Hit Start	Hit End	Description
Q3BYI0	34	745	31	742	1,4-alpha-glucan branching enzyme GlgB 2 OS=Xanthomonas campestris pv. vesicatoria (strain 85-10) OX=316273 GN=glgB2 PE=3 SV=1
Q8PDD1	34	745	17	728	1,4-alpha-glucan branching enzyme GlgB 2 OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=glgB2 PE=3 SV=1
Q2P9F7	34	745	31	743	1,4-alpha-glucan branching enzyme GlgB 1 OS=Xanthomonas oryzae pv. oryzae (strain MAFF 311018) OX=342109 GN=glgB1 PE=3 SV=1
Q4UZL7	34	745	17	728	1,4-alpha-glucan branching enzyme GlgB 2 OS=Xanthomonas campestris pv. campestris (strain 8004) OX=314565 GN=glgB2 PE=3 SV=1
Q5H6Q3	34	745	7	719	1,4-alpha-glucan branching enzyme GlgB 2 OS=Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) OX=291331 GN=glgB2 PE=3 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
0.999906	0.000090	0.000002	0.000000	0.000000	0.000002

TMHMM Annotations help

There is no transmembrane helices in MGYG000002381_03257.

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