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CAZyme Information: MGYG000002390_00343

You are here: Home > Sequence: MGYG000002390_00343

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 Ligilactobacillus agilis
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Ligilactobacillus; Ligilactobacillus agilis
CAZyme ID MGYG000002390_00343
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
649 MGYG000002390_11|CGC3 75715.8 6.7922
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002390 2133539 Isolate not provided not provided
Gene Location Start: 132311;  End: 134260  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 179 477 6.9e-138 0.9966777408637874
CBM48 27 111 2.6e-18 0.8947368421052632

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0296 GlgB 0.0 16 627 14 628
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK12313 PRK12313 0.0 16 631 15 631
1,4-alpha-glucan branching protein GlgB.
PRK05402 PRK05402 0.0 16 629 108 725
1,4-alpha-glucan branching protein GlgB.
PRK12568 PRK12568 0.0 16 626 115 727
glycogen branching enzyme; Provisional
cd11322 AmyAc_Glg_BE 0.0 115 511 2 400
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
ASR41991.1 0.0 6 649 1 644
AUJ31272.1 0.0 7 636 6 635
QYH54798.1 0.0 7 635 6 634
QCQ03558.1 0.0 8 633 6 628
AWZ38541.1 0.0 8 633 6 628

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JOY_A 4.41e-171 18 627 14 618
TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
1M7X_A 3.10e-170 15 625 1 612
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 5.73e-170 15 626 136 772
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]
5GR5_A 1.61e-169 15 626 136 772
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
4LPC_A 2.11e-169 25 625 6 607
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q1WSM8 0.0 15 638 20 645
1,4-alpha-glucan branching enzyme GlgB OS=Ligilactobacillus salivarius (strain UCC118) OX=362948 GN=glgB PE=3 SV=1
A3CM01 1.31e-309 8 626 2 619
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus sanguinis (strain SK36) OX=388919 GN=glgB PE=3 SV=1
A8AYH3 2.37e-309 8 626 2 619
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288) OX=467705 GN=glgB PE=3 SV=1
Q8DT52 2.11e-299 10 626 4 621
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=glgB PE=3 SV=1
Q04KG8 2.34e-297 8 626 2 619
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 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
1.000062 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002390_00343.