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CAZyme Information: MGYG000000028_01320

You are here: Home > Sequence: MGYG000000028_01320

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 Anaerostipes hadrus_A
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Anaerostipes; Anaerostipes hadrus_A
CAZyme ID MGYG000000028_01320
CAZy Family CBM48
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
726 MGYG000000028_4|CGC1 84620.86 6.8467
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000028 2458431 Isolate United Kingdom Europe
Gene Location Start: 67056;  End: 69236  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 176 477 3.5e-143 0.9966777408637874
CBM48 25 105 8.8e-18 0.868421052631579

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11322 AmyAc_Glg_BE 0.0 109 514 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.
TIGR01515 branching_enzym 0.0 9 636 1 618
alpha-1,4-glucan:alpha-1,4-glucan 6-glycosyltransferase. This model describes the glycogen branching enzymes which are responsible for the transfer of chains of approx. 7 alpha(1--4)-linked glucosyl residues to other similar chains (in new alpha(1--6) linkages) in the biosynthesis of glycogen. This enzyme is a member of the broader amylase family of starch hydrolases which fold as (beta/alpha)8 barrels, the so-called TIM-barrel structure. All of the sequences comprising the seed of this model have been experimentally characterized. This model encompasses both bacterial and eukaryotic species. No archaea have this enzyme, although Aquifex aolicus does. Two species, Bacillus thuringiensis and Clostridium perfringens have two sequences each which are annotated as amylases. These annotations are aparrently in error. GP|18143720 from C. perfringens, for instance, contains the note "674 aa, similar to gp:A14658_1 amylase (1,4-alpha-glucan branching enzyme (EC 2.4.1.18) ) from Bacillus thuringiensis (648 aa); 51.1% identity in 632 aa overlap." A branching enzyme from Porphyromonas gingivales, OMNI|PG1793, appears to be more closely related to the eukaryotic species (across a deep phylogenetic split) and may represent an instance of lateral transfer from this species' host. A sequence from Arabidopsis thaliana, GP|9294564, scores just above trusted, but appears either to contain corrupt sequence or, more likely, to be a pseudogene as some of the conserved catalytic residues common to the alpha amylase family are not conserved here. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
PRK14706 PRK14706 0.0 37 656 41 638
glycogen branching enzyme; Provisional
PRK14705 PRK14705 0.0 4 636 602 1221
glycogen branching enzyme; Provisional
PRK05402 PRK05402 0.0 4 638 99 724
1,4-alpha-glucan branching protein GlgB.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQP40138.1 0.0 1 656 1 657
CBL37815.1 0.0 1 656 1 657
QCP35773.1 0.0 1 652 1 658
QMW70941.1 0.0 1 651 1 657
BCD36168.1 0.0 1 651 1 657

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5GQW_A 1.68e-185 2 595 126 736
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 2.37e-185 2 595 126 736
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 2.37e-185 2 595 126 736
Crystalstructure of branching enzyme W610A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQZ_A 3.34e-185 2 595 126 736
Crystalstructure of branching enzyme Y500A mutant from Cyanothece sp. ATCC 51142 [Crocosphaera subtropica ATCC 51142]
5GQU_A 4.72e-185 2 595 126 736
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P30539 1.85e-208 5 604 7 604
1,4-alpha-glucan branching enzyme GlgB OS=Butyrivibrio fibrisolvens OX=831 GN=glgB PE=1 SV=1
Q21WG7 1.21e-205 9 597 6 586
1,4-alpha-glucan branching enzyme GlgB OS=Rhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) OX=338969 GN=glgB PE=3 SV=1
Q1AZ86 3.06e-204 9 634 103 716
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
B8CVY1 1.31e-203 9 636 10 626
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 1.20e-201 5 638 7 629
1,4-alpha-glucan branching enzyme GlgB OS=Aquifex aeolicus (strain VF5) OX=224324 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
1.000057 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000028_01320.