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CAZyme Information: MGYG000001335_01646

You are here: Home > Sequence: MGYG000001335_01646

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 Lactobacillus ultunensis
Lineage Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; Lactobacillus; Lactobacillus ultunensis
CAZyme ID MGYG000001335_01646
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
635 74479.95 8.111
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001335 2168092 Isolate not provided not provided
Gene Location Start: 252882;  End: 254789  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 172 472 1.2e-133 0.9966777408637874
CBM48 26 104 4.1e-18 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 0.0 108 508 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.
COG0296 GlgB 0.0 14 622 14 628
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK05402 PRK05402 0.0 14 622 108 723
1,4-alpha-glucan branching protein GlgB.
PRK12313 PRK12313 0.0 6 628 7 633
1,4-alpha-glucan branching protein GlgB.
PRK12568 PRK12568 0.0 37 621 142 727
glycogen branching enzyme; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QQP29541.1 0.0 4 635 1 632
QDD70718.1 0.0 1 635 1 635
AEA31645.1 0.0 1 635 1 635
ADZ06852.1 0.0 1 635 1 635
ADQ58679.1 0.0 1 635 1 635

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GQW_A 2.01e-169 14 625 137 778
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 3.18e-168 14 625 137 778
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQZ_A 4.49e-168 14 625 137 778
Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQU_A 6.34e-168 14 625 137 778
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]
5GR3_A 8.95e-168 14 625 137 778
Crystalstructure of branching enzyme L541A/W655A 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
Q5FL68 0.0 4 634 4 634
1,4-alpha-glucan branching enzyme GlgB OS=Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM) OX=272621 GN=glgB PE=3 SV=1
Q1WSM8 9.92e-290 14 634 21 644
1,4-alpha-glucan branching enzyme GlgB OS=Ligilactobacillus salivarius (strain UCC118) OX=362948 GN=glgB PE=3 SV=1
A8AYH3 6.55e-272 9 634 5 627
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 4.19e-271 9 634 5 627
1,4-alpha-glucan branching enzyme GlgB OS=Streptococcus sanguinis (strain SK36) OX=388919 GN=glgB PE=3 SV=1
Q8DT52 1.04e-269 5 633 1 628
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
1.000065 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001335_01646.