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CAZyme Information: MGYG000002527_01519

You are here: Home > Sequence: MGYG000002527_01519

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aeromonas caviae
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Aeromonadaceae; Aeromonas; Aeromonas caviae
CAZyme ID MGYG000002527_01519
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
725 82970.4 6.2711
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002527 4477475 Isolate Brazil South America
Gene Location Start: 77245;  End: 79422  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 273 573 3.7e-160 0.9966777408637874
CBM48 127 203 1e-16 0.8552631578947368

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK14706 PRK14706 0.0 116 722 25 620
glycogen branching enzyme; Provisional
PRK05402 PRK05402 0.0 3 725 6 725
1,4-alpha-glucan branching protein GlgB.
PRK14705 PRK14705 0.0 27 722 519 1221
glycogen branching enzyme; Provisional
PRK12313 PRK12313 0.0 113 724 22 628
1,4-alpha-glucan branching protein GlgB.
cd11322 AmyAc_Glg_BE 0.0 211 609 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDO77038.1 0.0 1 725 1 725
BDA12275.1 0.0 1 725 1 725
AUT43450.1 0.0 1 725 1 725
QLL83466.1 0.0 1 725 1 725
QUM02247.1 0.0 1 725 1 725

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4LPC_A 7.36e-240 115 725 6 611
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 8.78e-240 115 725 11 616
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]
5GQW_A 1.65e-227 13 724 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]
5GR0_A 3.31e-227 13 724 40 774
Crystalstructure of branching enzyme D501A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GR5_A 4.68e-227 13 724 40 774
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [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
Q9KNE8 0.0 4 722 15 725
1,4-alpha-glucan branching enzyme GlgB OS=Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) OX=243277 GN=glgB PE=3 SV=2
Q15VD0 0.0 4 721 5 724
1,4-alpha-glucan branching enzyme GlgB OS=Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087) OX=342610 GN=glgB PE=3 SV=1
Q6LHN1 0.0 1 721 1 710
1,4-alpha-glucan branching enzyme GlgB OS=Photobacterium profundum (strain SS9) OX=298386 GN=glgB PE=3 SV=1
Q7MG90 0.0 4 722 3 713
1,4-alpha-glucan branching enzyme GlgB OS=Vibrio vulnificus (strain YJ016) OX=196600 GN=glgB PE=3 SV=2
Q8D4P0 2.83e-318 4 722 3 713
1,4-alpha-glucan branching enzyme GlgB OS=Vibrio vulnificus (strain CMCP6) OX=216895 GN=glgB PE=3 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 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002527_01519.