logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001854_00878

You are here: Home > Sequence: MGYG000001854_00878

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; Borkfalkiaceae; UBA11940;
CAZyme ID MGYG000001854_00878
CAZy Family GH13
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
682 79562.34 6.3347
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001854 1440109 MAG Denmark Europe
Gene Location Start: 3838;  End: 5886  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 181 478 9.1e-134 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 7 622 101 724
1,4-alpha-glucan branching protein GlgB.
PRK14705 PRK14705 0.0 7 622 604 1222
glycogen branching enzyme; Provisional
PRK12313 PRK12313 0.0 5 620 6 626
1,4-alpha-glucan branching protein GlgB.
cd11322 AmyAc_Glg_BE 0.0 113 514 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 7 621 7 628
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
QRP41890.1 1.22e-228 5 619 20 640
ASN93451.1 1.22e-228 5 619 20 640
CBL36213.1 5.84e-228 5 619 33 655
QJU22196.1 1.40e-227 5 619 20 640
CBK76102.1 1.34e-226 5 619 33 655

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GR1_A 2.38e-190 10 621 133 773
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]
5GQZ_A 2.38e-190 10 621 133 773
Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQW_A 6.73e-190 10 621 133 773
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]
5GR2_A 9.52e-190 10 621 133 773
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]
5GR5_A 9.52e-190 10 621 133 773
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
P30539 1.29e-215 2 619 3 630
1,4-alpha-glucan branching enzyme GlgB OS=Butyrivibrio fibrisolvens OX=831 GN=glgB PE=1 SV=1
Q8DLB8 7.43e-199 8 584 108 706
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
O66936 3.18e-198 8 584 9 584
1,4-alpha-glucan branching enzyme GlgB OS=Aquifex aeolicus (strain VF5) OX=224324 GN=glgB PE=3 SV=1
Q1AZ86 2.33e-197 8 617 101 715
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 5.32e-196 8 619 105 726
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
1.000048 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001854_00878.