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CAZyme Information: MGYG000002319_00433

You are here: Home > Sequence: MGYG000002319_00433

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 Limosilactobacillus mucosae
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Limosilactobacillus; Limosilactobacillus mucosae
CAZyme ID MGYG000002319_00433
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
657 MGYG000002319_7|CGC4 76294.15 6.6891
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002319 2369669 Isolate not provided not provided
Gene Location Start: 133530;  End: 135503  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 177 475 4.8e-131 0.9966777408637874
CBM48 26 108 4.6e-18 0.868421052631579

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK05402 PRK05402 0.0 1 628 99 726
1,4-alpha-glucan branching protein GlgB.
PRK14705 PRK14705 0.0 16 626 613 1223
glycogen branching enzyme; Provisional
PRK12313 PRK12313 0.0 1 630 6 632
1,4-alpha-glucan branching protein GlgB.
cd11322 AmyAc_Glg_BE 0.0 112 509 1 400
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.
COG0296 GlgB 0.0 17 625 17 628
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QLI94452.1 0.0 1 657 1 657
QOL69601.1 0.0 1 657 1 655
AJT50360.1 0.0 1 657 1 655
QXL49060.1 0.0 4 634 11 640
ATP36875.1 0.0 4 634 11 640

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JOY_A 3.86e-177 2 625 4 618
TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
5GQW_A 1.18e-168 14 624 137 772
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 3.33e-168 14 624 137 772
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQZ_A 4.70e-168 14 624 137 772
Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQU_A 6.64e-168 14 624 137 772
Crystalstructure of branching enzyme from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GQV_A Crystal structure of branching enzyme from Cyanothece sp. ATCC 51142 in complex with maltohexaose [Crocosphaera subtropica ATCC 51142],5GQY_A Crystal structure of branching enzyme 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
Q1WSM8 0.0 4 634 11 640
1,4-alpha-glucan branching enzyme GlgB OS=Ligilactobacillus salivarius (strain UCC118) OX=362948 GN=glgB PE=3 SV=1
A8AYH3 6.71e-292 6 630 2 625
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 5.28e-290 10 624 6 621
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=glgB PE=3 SV=1
Q5FL68 6.19e-289 1 634 1 630
1,4-alpha-glucan branching enzyme GlgB OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=glgB PE=3 SV=1
A3CM01 1.34e-287 6 624 2 619
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus sanguinis (strain SK36) OX=388919 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
1.000068 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002319_00433.