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CAZyme Information: MGYG000001208_02129

You are here: Home > Sequence: MGYG000001208_02129

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 Enterococcus_C dispar
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_C; Enterococcus_C dispar
CAZyme ID MGYG000001208_02129
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
646 75542.63 6.1614
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001208 2570475 MAG Austria Europe
Gene Location Start: 6057;  End: 7997  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 176 474 1.5e-137 0.9966777408637874
CBM48 29 108 1.5e-17 0.881578947368421

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11322 AmyAc_Glg_BE 0.0 112 510 2 402
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 0.0 17 626 108 725
1,4-alpha-glucan branching protein GlgB.
PRK12313 PRK12313 0.0 13 630 11 633
1,4-alpha-glucan branching protein GlgB.
COG0296 GlgB 0.0 17 624 14 628
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
TIGR01515 branching_enzym 0.0 17 623 5 618
alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase. This model describes the glycogen branching enzymes which are responsible for the transfer of chains of approx. 7 alpha(1--4)-linked glucosyl residues to other similar chains (in new alpha(1--6) linkages) in the biosynthesis of glycogen. This enzyme is a member of the broader amylase family of starch hydrolases which fold as (beta/alpha)8 barrels, the so-called TIM-barrel structure. All of the sequences comprising the seed of this model have been experimentally characterized. This model encompasses both bacterial and eukaryotic species. No archaea have this enzyme, although Aquifex aolicus does. Two species, Bacillus thuringiensis and Clostridium perfringens have two sequences each which are annotated as amylases. These annotations are aparrently in error. GP|18143720 from C. perfringens, for instance, contains the note "674 aa, similar to gp:A14658_1 amylase (1,4-alpha-glucan branching enzyme (EC 2.4.1.18) ) from Bacillus thuringiensis (648 aa); 51.1% identity in 632 aa overlap." A branching enzyme from Porphyromonas gingivales, OMNI|PG1793, appears to be more closely related to the eukaryotic species (across a deep phylogenetic split) and may represent an instance of lateral transfer from this species' host. A sequence from Arabidopsis thaliana, GP|9294564, scores just above trusted, but appears either to contain corrupt sequence or, more likely, to be a pseudogene as some of the conserved catalytic residues common to the alpha amylase family are not conserved here. [Energy metabolism, Biosynthesis and degradation of polysaccharides]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCA86029.1 0.0 1 646 1 644
QCT93389.1 0.0 10 634 1 625
QOG29128.1 0.0 10 634 1 625
QGR83541.1 0.0 10 634 1 625
AYY11243.1 0.0 10 634 1 625

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JOY_A 4.09e-168 16 625 11 619
TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
5GQW_A 1.28e-164 4 623 115 772
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 3.60e-164 4 623 115 772
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GR1_A 3.60e-164 4 623 115 772
Crystalstructure of branching enzyme Y500A/D501A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142],5GR6_A Crystal structure of branching enzyme Y500A/D501A double mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GR0_A 5.09e-164 4 623 115 772
Crystalstructure of branching enzyme D501A 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
Q1WSM8 0.0 17 641 21 649
1,4-alpha-glucan branching enzyme GlgB OS=Ligilactobacillus salivarius (strain UCC118) OX=362948 GN=glgB PE=3 SV=1
A8AYH3 5.01e-315 8 635 1 628
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
A3CM01 5.60e-315 8 623 1 619
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus sanguinis (strain SK36) OX=388919 GN=glgB PE=3 SV=1
Q5FL68 1.03e-308 1 640 4 638
1,4-alpha-glucan branching enzyme GlgB OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=glgB PE=3 SV=1
Q8DT52 2.23e-305 17 623 10 621
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) OX=210007 GN=glgB PE=3 SV=1

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
1.000072 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001208_02129.