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CAZyme Information: MGYG000003507_01099

You are here: Home > Sequence: MGYG000003507_01099

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 UBA733 sp900767825
Lineage Bacteria; Firmicutes; Bacilli; RFN20; CAG-826; UBA733; UBA733 sp900767825
CAZyme ID MGYG000003507_01099
CAZy Family GH13
CAZyme Description Glycogen debranching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1045 118001.04 4.8844
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003507 1599809 MAG Fiji Oceania
Gene Location Start: 29876;  End: 33013  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1 3.2.1.41

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 504 842 6.4e-86 0.9930795847750865

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02104 pulA_typeI 1.35e-149 309 923 3 528
pullulanase, type I. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. This family consists of pullulanases related to the subfamilies described in TIGR02102 and TIGR02103 but having a different domain architecture with shorter sequences. Members are called type I pullulanases.
cd11341 AmyAc_Pullulanase_LD-like 1.93e-143 461 921 5 406
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.
COG1523 PulA 8.24e-93 332 923 69 587
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877 PLN02877 5.85e-70 312 855 209 787
alpha-amylase/limit dextrinase
TIGR02102 pullulan_Gpos 8.22e-65 68 910 112 875
pullulanase, extracellular, Gram-positive. Pullulan is an unusual, industrially important polysaccharide in which short alpha-1,4 chains (maltotriose) are connected in alpha-1,6 linkages. Enzymes that cleave alpha-1,6 linkages in pullulan and release maltotriose are called pullulanases although pullulan itself may not be the natural substrate. In contrast, a glycogen debranching enzyme such GlgX, homologous to this family, can release glucose at alpha,1-6 linkages from glycogen first subjected to limit degradation by phosphorylase. Characterized members of this family include a surface-located pullulanase from Streptococcus pneumoniae () and an extracellular bifunctional amylase/pullulanase with C-terminal pullulanase activity (.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEU81131.1 1.77e-115 69 922 31 792
VEU82346.1 5.47e-109 67 921 28 788
QWB95757.1 1.55e-106 267 922 198 796
QLY39684.1 1.40e-103 70 923 73 832
QOS39053.1 2.04e-100 3 847 2 759

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6JEQ_A 2.00e-80 312 923 34 560
Crystalstructure of Pullulanase from Paenibacillus barengoltzii complex with beta-cyclodextrin [Paenibacillus barengoltzii],6JFJ_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin [Paenibacillus barengoltzii],6JFX_A Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltopentaose [Paenibacillus barengoltzii],6JHF_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii [Paenibacillus barengoltzii],6JHG_A Crystal structure of apo Pullulanase from Paenibacillus barengoltzii in space group P212121 [Paenibacillus barengoltzii]
2WAN_A 2.32e-80 70 921 7 824
Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]
6JHI_A 2.58e-79 312 923 34 560
Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]
6JHH_A 2.58e-79 312 923 34 560
Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
7LSA_A 2.67e-77 311 924 56 620
ChainA, Pullulanase [Ruminococcus bromii]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O33840 1.72e-76 312 922 219 746
Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0 3.67e-69 294 923 82 615
Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
Q9F930 5.75e-54 68 915 251 1023
Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2UNG0 7.54e-54 68 915 244 1016
Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
A0A0H2ZL64 1.28e-53 68 915 229 1001
Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000001 1.000079 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003507_01099.