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CAZyme Information: MGYG000001484_00868

You are here: Home > Sequence: MGYG000001484_00868

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 Nigerium massiliense
Lineage Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Nigerium; Nigerium massiliense
CAZyme ID MGYG000001484_00868
CAZy Family GH13
CAZyme Description Isoamylase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
808 89857.67 5.0338
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001484 2934258 Isolate not provided not provided
Gene Location Start: 618886;  End: 621312  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 254 611 5e-114 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 4.60e-157 200 612 1 392
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.
COG1523 PulA 2.43e-132 39 803 19 689
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PRK03705 PRK03705 5.73e-113 39 753 11 624
glycogen debranching protein GlgX.
PRK14510 PRK14510 4.54e-87 39 633 15 551
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
cd11341 AmyAc_Pullulanase_LD-like 1.21e-45 216 611 5 367
Alpha amylase catalytic domain found in Pullulanase (also called dextrinase; alpha-dextrin endo-1,6-alpha glucosidase), limit dextrinase, and related proteins. Pullulanase is an enzyme with action similar to that of isoamylase; it cleaves 1,6-alpha-glucosidic linkages in pullulan, amylopectin, and glycogen, and in alpha-and beta-amylase limit-dextrins of amylopectin and glycogen. Pullulanases are very similar to limit dextrinases, although they differ in their action on glycogen and the rate of hydrolysis of 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QTE25891.1 0.0 32 806 12 781
QIK72013.1 0.0 25 806 4 777
QQM67598.1 2.59e-302 32 802 11 769
VEG55497.1 1.09e-301 25 802 4 770
SNV18689.1 4.77e-300 29 775 24 817

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1BF2_A 3.98e-130 40 773 7 714
StructureOf Pseudomonas Isoamylase [Pseudomonas amyloderamosa]
2VNC_A 7.97e-96 38 630 18 568
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 1.73e-81 39 635 11 545
Crystalstructure of Glycogen Debranching Enzyme GlgX from Escherichia coli K-12 [Escherichia coli K-12]
4J7R_A 6.50e-67 39 634 64 686
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]
3WDH_A 2.09e-28 195 620 198 584
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
O32611 6.59e-133 40 775 39 743
Isoamylase OS=Flavobacterium sp. OX=239 GN=iam PE=1 SV=1
P10342 4.39e-129 40 773 33 740
Isoamylase OS=Pseudomonas amyloderamosa OX=32043 GN=iam PE=1 SV=3
P26501 1.71e-128 40 773 33 740
Isoamylase OS=Pseudomonas sp. (strain SMP1) OX=72588 GN=iam PE=1 SV=1
P9WQ25 1.68e-96 30 752 17 676
Glycogen operon protein GlgX homolog OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=glgX PE=1 SV=1
P9WQ24 1.68e-96 30 752 17 676
Glycogen operon protein GlgX homolog OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=glgX 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
0.999366 0.000679 0.000010 0.000001 0.000001 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001484_00868.