logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000000028_00673

You are here: Home > Sequence: MGYG000000028_00673

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_00673
CAZy Family GH13
CAZyme Description Glycogen debranching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
713 MGYG000000028_2|CGC5 81924.1 5.0907
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000028 2458431 Isolate United Kingdom Europe
Gene Location Start: 185402;  End: 187543  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.68 3.2.1.- 2.4.1.25

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 188 549 1.7e-150 0.9971509971509972

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11326 AmyAc_Glg_debranch 0.0 152 591 1 433
Alpha amylase catalytic domain found in glycogen debranching enzymes. Debranching enzymes facilitate the breakdown of glycogen through glucosyltransferase and glucosidase activity. These activities are performed by a single enzyme in mammals, yeast, and some bacteria, but by two distinct enzymes in Escherichia coli and other bacteria. Debranching enzymes perform two activities: 4-alpha-D-glucanotransferase (EC 2.4.1.25) and amylo-1,6-glucosidase (EC 3.2.1.33). 4-alpha-D-glucanotransferase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. Amylo-alpha-1,6-glucosidase catalyzes the endohydrolysis of 1,6-alpha-D-glucoside linkages at points of branching in chains of 1,4-linked alpha-D-glucose residues. In Escherichia coli, GlgX is the debranching enzyme and malQ is the 4-alpha-glucanotransferase. TreX, an archaeal glycogen-debranching enzyme has dual activities like mammals and yeast, but is structurally similar to GlgX. TreX exists in two oligomeric states, a dimer and tetramer. Isoamylase (EC 3.2.1.68) is one of the starch-debranching enzymes that catalyzes the hydrolysis of alpha-1,6-glucosidic linkages specific in alpha-glucans such as amylopectin or glycogen and their beta-limit dextrins. 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.
TIGR02100 glgX_debranch 0.0 37 708 8 688
glycogen debranching enzyme GlgX. This family consists of the GlgX protein from the E. coli glycogen operon and probable equivalogs from other prokaryotic species. GlgX is not required for glycogen biosynthesis, but instead acts as a debranching enzyme for glycogen catabolism. This model distinguishes GlgX from pullanases and other related proteins that also operate on alpha-1,6-glycosidic linkages. In the wide band between the trusted and noise cutoffs are functionally similar enzymes, mostly from plants, that act similarly but usually are termed isoamylase. [Energy metabolism, Biosynthesis and degradation of polysaccharides]
COG1523 PulA 0.0 44 713 31 696
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PRK03705 PRK03705 1.55e-159 20 596 1 566
glycogen debranching protein GlgX.
PRK14510 PRK14510 4.61e-153 28 660 8 647
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AQP40888.1 0.0 16 713 1 698
CBL24510.1 0.0 19 709 18 708
QCU02983.1 0.0 10 709 9 708
CBL18519.1 0.0 10 709 9 708
ADD61706.1 0.0 10 709 9 708

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4J7R_A 5.45e-139 45 596 76 711
CrystalStructure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) [Chlamydomonas reinhardtii],4J7R_B Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) [Chlamydomonas reinhardtii],4OKD_A Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) in complex with maltoheptaose [Chlamydomonas reinhardtii],4OKD_B Crystal Structure of Chlamydomonas reinhardtii Isoamylase 1 (ISA1) in complex with maltoheptaose [Chlamydomonas reinhardtii]
2VNC_A 8.74e-131 44 675 30 686
Crystalstructure of Glycogen Debranching enzyme TreX from Sulfolobus solfataricus [Saccharolobus solfataricus],2VNC_B Crystal structure of Glycogen Debranching enzyme TreX from Sulfolobus solfataricus [Saccharolobus solfataricus],2VR5_A Crystal structure of Trex from Sulfolobus Solfataricus in complex with acarbose intermediate and glucose [Saccharolobus solfataricus],2VR5_B Crystal structure of Trex from Sulfolobus Solfataricus in complex with acarbose intermediate and glucose [Saccharolobus solfataricus],2VUY_A Crystal structure of Glycogen Debranching exzyme TreX from Sulfolobus solfatarius [Saccharolobus solfataricus],2VUY_B Crystal structure of Glycogen Debranching exzyme TreX from Sulfolobus solfatarius [Saccharolobus solfataricus],7EAV_A Chain A, Glycogen debranching enzyme [Saccharolobus solfataricus],7EAV_B Chain B, Glycogen debranching enzyme [Saccharolobus solfataricus]
2WSK_A 3.15e-94 37 679 13 638
Crystalstructure of Glycogen Debranching Enzyme GlgX from Escherichia coli K-12 [Escherichia coli K-12]
1BF2_A 3.71e-64 109 674 105 711
StructureOf Pseudomonas Isoamylase [Pseudomonas amyloderamosa]
3WDH_A 1.35e-43 47 595 122 621
Crystalstructure of Pullulanase from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDI_A Crystal structure of Pullulanase complexed with maltotriose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11],3WDJ_A Crystal structure of Pullulanase complexed with maltotetraose from Anoxybacillus sp. LM18-11 [Anoxybacillus sp. LM18-11]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q9M0S5 1.19e-151 20 674 77 731
Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2
B9G434 2.10e-147 37 674 109 748
Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
O04196 1.32e-145 11 674 52 733
Isoamylase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA1 PE=1 SV=1
O22637 1.05e-142 37 674 89 741
Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
D0TZF0 3.05e-142 37 674 105 755
Isoamylase 1, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA1 PE=1 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
1.000058 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000028_00673.