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CAZyme Information: MGYG000001543_01898

You are here: Home > Sequence: MGYG000001543_01898

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 sp900078195
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lachnoclostridium; Lachnoclostridium sp900078195
CAZyme ID MGYG000001543_01898
CAZy Family GH13
CAZyme Description Glycogen debranching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
668 MGYG000001543_7|CGC3 78260.82 6.8108
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001543 4599950 Isolate not provided not provided
Gene Location Start: 263301;  End: 265307  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001543_01898.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 278 469 5.5e-55 0.6011396011396012

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11326 AmyAc_Glg_debranch 4.22e-138 122 511 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 1.49e-120 12 615 4 675
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 5.50e-116 4 602 9 668
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PRK03705 PRK03705 8.38e-85 85 510 90 560
glycogen debranching protein GlgX.
PRK14510 PRK14510 1.46e-72 14 588 15 647
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBF41510.1 4.40e-200 14 602 18 605
BCN30257.1 1.36e-193 13 605 13 609
ADL06627.1 9.11e-175 8 607 9 580
QRV19300.1 9.11e-175 8 607 9 580
SEU00412.1 3.53e-174 15 607 16 580

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2VNC_A 7.74e-67 14 602 19 685
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]
4J7R_A 6.88e-60 14 611 64 789
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]
2WSK_A 4.54e-50 85 510 90 560
Crystalstructure of Glycogen Debranching Enzyme GlgX from Escherichia coli K-12 [Escherichia coli K-12]
1BF2_A 5.56e-29 129 596 171 705
StructureOf Pseudomonas Isoamylase [Pseudomonas amyloderamosa]
3WDH_A 2.46e-25 2 515 98 621
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
O22637 1.37e-80 14 613 87 752
Isoamylase SU1, chloroplastic OS=Zea mays OX=4577 GN=SU1 PE=1 SV=1
O04196 8.81e-80 14 609 76 740
Isoamylase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA1 PE=1 SV=1
D0TZF0 3.38e-79 14 614 103 767
Isoamylase 1, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA1 PE=1 SV=1
B9G434 7.72e-72 14 518 107 683
Isoamylase 3, chloroplastic OS=Oryza sativa subsp. japonica OX=39947 GN=ISA3 PE=2 SV=1
Q9M0S5 4.03e-71 9 613 87 742
Isoamylase 3, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=ISA3 PE=1 SV=2

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 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001543_01898.