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CAZyme Information: MGYG000002417_02015

You are here: Home > Sequence: MGYG000002417_02015

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 Lachnoclostridium_A edouardi
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium_A; Lachnoclostridium_A edouardi
CAZyme ID MGYG000002417_02015
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
798 MGYG000002417_1|CGC15 91003.75 6.6361
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002417 3329949 Isolate not provided not provided
Gene Location Start: 2159281;  End: 2161677  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 292 592 2.7e-151 0.9933554817275747
CBM48 127 212 2e-17 0.8947368421052632

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG0296 GlgB 0.0 103 741 1 627
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK14705 PRK14705 0.0 9 740 503 1220
glycogen branching enzyme; Provisional
PRK12313 PRK12313 0.0 106 740 5 625
1,4-alpha-glucan branching protein GlgB.
PRK05402 PRK05402 0.0 21 740 11 721
1,4-alpha-glucan branching protein GlgB.
cd11322 AmyAc_Glg_BE 0.0 215 628 1 402
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CBK76766.1 0.0 1 757 1 759
CBL36572.1 0.0 1 757 1 759
QRV19504.1 0.0 1 761 1 764
ADL06402.1 0.0 1 761 1 764
SET97328.1 0.0 1 744 1 744

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GQW_A 5.01e-267 14 744 30 775
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 8.12e-266 14 744 30 775
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQZ_A 1.15e-265 14 744 30 775
Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQU_A 1.63e-265 14 744 30 775
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]
6KLF_A 7.15e-265 14 744 6 751
ChainA, 1,4-alpha-glucan branching enzyme GlgB [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
Q8DLB8 5.83e-269 14 739 8 747
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
P52981 6.20e-267 14 739 10 749
1,4-alpha-glucan branching enzyme GlgB OS=Synechocystis sp. (strain PCC 6803 / Kazusa) OX=1111708 GN=glgB PE=3 SV=1
P16954 2.59e-259 14 739 17 756
1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus elongatus (strain PCC 7942 / FACHB-805) OX=1140 GN=glgB PE=1 SV=2
Q5N4W5 2.59e-259 14 739 17 756
1,4-alpha-glucan branching enzyme GlgB OS=Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) OX=269084 GN=glgB PE=3 SV=1
Q1AZ86 4.94e-259 14 736 7 713
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

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
1.000070 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002417_02015.