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CAZyme Information: MGYG000003559_00974

You are here: Home > Sequence: MGYG000003559_00974

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 HGM04593 sp900769765
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; HGM04593; HGM04593 sp900769765
CAZyme ID MGYG000003559_00974
CAZy Family GH13
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
668 77758.32 6.8392
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003559 1756049 MAG Fiji Oceania
Gene Location Start: 10023;  End: 12029  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 217 508 5.4e-145 0.9965870307167235

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11321 AmyAc_bac_euk_BE 0.0 148 552 1 406
Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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.
PLN02447 PLN02447 0.0 1 662 59 727
1,4-alpha-glucan-branching enzyme
PLN02960 PLN02960 7.26e-164 96 664 326 890
alpha-amylase
PLN03244 PLN03244 4.33e-136 96 664 331 865
alpha-amylase; Provisional
COG0296 GlgB 2.02e-105 47 664 23 627
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
QRQ47593.1 0.0 2 667 4 669
QUT46852.1 0.0 2 667 4 669
ASM66816.1 0.0 2 667 5 670
QUU09288.1 0.0 2 667 5 670
QQT76584.1 0.0 2 667 5 670

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BZY_A 4.88e-207 1 663 28 695
Crystalstructure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_B Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens],4BZY_C Crystal structure of human glycogen branching enzyme (GBE1) [Homo sapiens]
5CLT_A 7.56e-203 11 663 6 663
Crystalstructure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLT_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with acarbose [Homo sapiens],5CLW_A Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_B Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens],5CLW_C Crystal structure of human glycogen branching enzyme (GBE1) in complex with maltoheptaose [Homo sapiens]
3AMK_A 3.78e-190 1 637 1 658
Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]
3VU2_A 1.07e-189 1 637 1 658
Structureof the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group],3VU2_B Structure of the Starch Branching Enzyme I (BEI) complexed with maltopentaose from Oryza sativa L [Oryza sativa Japonica Group]
3AML_A 2.04e-189 1 637 1 658
Structureof the Starch Branching Enzyme I (BEI) from Oryza sativa L [Oryza sativa Japonica Group]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q555Q9 1.63e-209 3 665 12 676
1,4-alpha-glucan-branching enzyme OS=Dictyostelium discoideum OX=44689 GN=glgB PE=3 SV=1
Q6EAS5 1.86e-208 3 663 27 692
1,4-alpha-glucan-branching enzyme OS=Equus caballus OX=9796 GN=GBE1 PE=1 SV=1
Q8NKE1 6.23e-208 8 663 20 680
1,4-alpha-glucan-branching enzyme OS=Rhizophagus irregularis (strain DAOM 181602 / DAOM 197198 / MUCL 43194) OX=747089 GN=GLC3 PE=2 SV=2
Q04446 9.41e-207 1 663 28 695
1,4-alpha-glucan-branching enzyme OS=Homo sapiens OX=9606 GN=GBE1 PE=1 SV=3
Q6T308 1.71e-206 1 663 25 692
1,4-alpha-glucan-branching enzyme OS=Felis catus OX=9685 GN=GBE1 PE=2 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
1.000059 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003559_00974.