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CAZyme Information: MGYG000003931_00902

You are here: Home > Sequence: MGYG000003931_00902

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
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-552; UMGS1880;
CAZyme ID MGYG000003931_00902
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
651 MGYG000003931_7|CGC2 76264.95 6.0522
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003931 1842922 MAG United Kingdom Europe
Gene Location Start: 73393;  End: 75348  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 173 470 6.3e-151 0.9933554817275747
CBM48 22 103 1.5e-17 0.868421052631579

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0296 GlgB 0.0 7 608 11 622
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK14705 PRK14705 0.0 35 578 642 1184
glycogen branching enzyme; Provisional
PRK12313 PRK12313 0.0 8 612 13 625
1,4-alpha-glucan branching protein GlgB.
cd11322 AmyAc_Glg_BE 0.0 108 506 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 8 616 106 724
1,4-alpha-glucan branching protein GlgB.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QOX62812.1 1.00e-243 8 624 12 638
CBL01646.1 7.10e-243 8 635 18 654
AXB29737.1 2.48e-242 8 640 18 659
ATL90043.1 1.22e-240 8 638 18 658
QIA41789.1 1.72e-240 8 638 18 658

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GQW_A 6.79e-201 8 568 135 722
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]
5GR1_A 6.79e-201 8 568 135 722
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]
5GR2_A 9.60e-201 8 568 135 722
Crystalstructure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142],5GR4_A Crystal structure of branching enzyme L541A mutant from Cyanothece sp. ATCC 51142 in complex with maltoheptaose [Crocosphaera subtropica ATCC 51142]
5GR0_A 9.60e-201 8 568 135 722
Crystalstructure of branching enzyme D501A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQZ_A 9.60e-201 8 568 135 722
Crystalstructure of branching enzyme Y500A 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
B8CVY1 5.89e-214 7 612 11 625
1,4-alpha-glucan branching enzyme GlgB OS=Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562) OX=373903 GN=glgB PE=3 SV=1
O66936 8.34e-214 8 608 13 622
1,4-alpha-glucan branching enzyme GlgB OS=Aquifex aeolicus (strain VF5) OX=224324 GN=glgB PE=3 SV=1
Q2JT08 9.62e-214 7 575 122 709
1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain JA-3-3Ab) OX=321327 GN=glgB PE=3 SV=1
Q2JK68 2.27e-210 7 575 122 709
1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain JA-2-3B'a(2-13)) OX=321332 GN=glgB PE=3 SV=1
Q8DLB8 5.69e-209 10 575 114 706
1,4-alpha-glucan branching enzyme GlgB OS=Thermosynechococcus vestitus (strain IAM M-273 / NIES-2133 / BP-1) OX=197221 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 MGYG000003931_00902.