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CAZyme Information: MGYG000002551_01342

You are here: Home > Sequence: MGYG000002551_01342

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 Haemophilus_A paraphrohaemolyticus
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Pasteurellaceae; Haemophilus_A; Haemophilus_A paraphrohaemolyticus
CAZyme ID MGYG000002551_01342
CAZy Family GH13
CAZyme Description 1,4-alpha-glucan branching enzyme GlgB
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
280 32098.12 5.3627
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002551 1748237 MAG China Asia
Gene Location Start: 59;  End: 901  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.18

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 3 125 2.5e-66 0.4053156146179402

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK05402 PRK05402 0.0 3 280 451 725
1,4-alpha-glucan branching protein GlgB.
PRK12313 PRK12313 1.38e-155 3 280 355 629
1,4-alpha-glucan branching protein GlgB.
TIGR01515 branching_enzym 2.51e-144 3 277 347 618
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]
COG0296 GlgB 9.87e-139 3 277 350 627
1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism].
PRK12568 PRK12568 4.85e-126 3 277 455 727
glycogen branching enzyme; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEH68147.1 1.27e-193 1 280 308 587
AXP40071.1 4.77e-192 1 280 450 729
BBE93385.1 4.77e-192 1 280 450 729
AKA47353.1 4.77e-192 1 280 450 729
AXP54832.1 4.77e-192 1 280 450 729

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4LPC_A 2.02e-136 1 276 334 607
CrystalStructure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_B Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_C Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LPC_D Crystal Structure of E.Coli Branching Enzyme in complex with maltoheptaose [Escherichia coli],4LQ1_A Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_B Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_C Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],4LQ1_D Crystal Structure of E.Coli Branching Enzyme in complex with maltohexaose [Escherichia coli],5E6Y_A Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_B Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_C Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Y_D Crystal structure of E.Coli branching enzyme in complex with alpha cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_A Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_B Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_C Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E6Z_D Crystal structure of Ecoli Branching Enzyme with beta cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_A Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_B Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_C Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A],5E70_D Crystal structure of Ecoli Branching Enzyme with gamma cyclodextrin [Escherichia coli O139:H28 str. E24377A]
1M7X_A 2.34e-136 1 276 339 612
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]
6JOY_A 1.12e-96 4 277 351 617
TheX-ray Crystallographic Structure of Branching Enzyme from Rhodothermus obamensis STB05 [Rhodothermus marinus]
3K1D_A 8.44e-92 3 276 449 719
Crystalstructure of glycogen branching enzyme synonym: 1,4-alpha-D-glucan:1,4-alpha-D-GLUCAN 6-glucosyl-transferase from mycobacterium tuberculosis H37RV [Mycobacterium tuberculosis H37Rv]
5GQW_A 4.54e-87 3 277 501 772
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q4QK67 9.55e-193 1 280 450 729
1,4-alpha-glucan branching enzyme GlgB OS=Haemophilus influenzae (strain 86-028NP) OX=281310 GN=glgB PE=3 SV=1
P45177 1.92e-192 1 279 450 728
1,4-alpha-glucan branching enzyme GlgB OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=glgB PE=3 SV=1
A5UEJ2 1.78e-190 1 280 450 729
1,4-alpha-glucan branching enzyme GlgB OS=Haemophilus influenzae (strain PittGG) OX=374931 GN=glgB PE=3 SV=1
Q9CN94 4.97e-172 3 280 452 729
1,4-alpha-glucan branching enzyme GlgB OS=Pasteurella multocida (strain Pm70) OX=272843 GN=glgB PE=3 SV=1
Q0I3H7 6.16e-158 3 277 452 726
1,4-alpha-glucan branching enzyme GlgB OS=Haemophilus somnus (strain 129Pt) OX=205914 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
1.000033 0.000005 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002551_01342.