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CAZyme Information: MGYG000000748_00578

You are here: Home > Sequence: MGYG000000748_00578

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 UBA10677 sp900762945
Lineage Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-552; UBA10677; UBA10677 sp900762945
CAZyme ID MGYG000000748_00578
CAZy Family GH13
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
621 MGYG000000748_11|CGC1 71522.7 6.6522
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000748 1946382 MAG Kazakhstan Asia
Gene Location Start: 16573;  End: 18438  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 168 468 1.3e-148 0.9966777408637874

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK05402 PRK05402 0.0 9 613 108 724
1,4-alpha-glucan branching protein GlgB.
PRK14705 PRK14705 0.0 37 573 645 1179
glycogen branching enzyme; Provisional
PRK12313 PRK12313 0.0 9 610 15 625
1,4-alpha-glucan branching protein GlgB.
cd11322 AmyAc_Glg_BE 0.0 106 503 4 401
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 9 610 14 626
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
CBL01646.1 1.42e-254 9 609 20 630
QIA41789.1 1.09e-253 9 609 20 630
ATO99826.1 1.09e-253 9 609 20 630
ATL90043.1 2.20e-253 9 609 20 630
AXB29737.1 2.93e-253 9 609 20 630

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JOY_A 6.52e-185 1 610 4 616
TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
1M7X_A 3.25e-184 11 613 4 615
TheX-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_B The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_C The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli],1M7X_D The X-ray Crystallographic Structure of Branching Enzyme [Escherichia coli]
5GQZ_A 6.81e-184 9 593 137 743
Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQW_A 6.81e-184 9 593 137 743
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 9.62e-184 9 593 137 743
Crystalstructure of branching enzyme W610A 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 1.61e-208 9 614 14 629
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
Q5NXV7 5.04e-201 9 611 18 626
1,4-alpha-glucan branching enzyme GlgB OS=Aromatoleum aromaticum (strain EbN1) OX=76114 GN=glgB PE=3 SV=1
O66936 1.08e-198 9 610 15 626
1,4-alpha-glucan branching enzyme GlgB OS=Aquifex aeolicus (strain VF5) OX=224324 GN=glgB PE=3 SV=1
Q1AZ86 1.80e-196 9 610 107 717
1,4-alpha-glucan branching enzyme GlgB OS=Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1) OX=266117 GN=glgB PE=3 SV=1
Q7NL20 5.82e-195 9 605 111 721
1,4-alpha-glucan branching enzyme GlgB OS=Gloeobacter violaceus (strain ATCC 29082 / PCC 7421) OX=251221 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
1.000046 0.000002 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000748_00578.