logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000004538_00083

You are here: Home > Sequence: MGYG000004538_00083

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 CAG-313 sp900760745
Lineage Bacteria; Firmicutes; Bacilli; ML615J-28; CAG-313; CAG-313; CAG-313 sp900760745
CAZyme ID MGYG000004538_00083
CAZy Family GH13
CAZyme Description Pullulanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
674 MGYG000004538_1|CGC2 79069.03 5.7183
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004538 1759821 MAG Israel Asia
Gene Location Start: 92443;  End: 94467  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004538_00083.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 244 546 1.7e-89 0.9896193771626297

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02104 pulA_typeI 1.22e-177 90 622 2 564
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 7.03e-165 205 586 1 406
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 1.84e-99 104 592 62 591
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
PLN02877 PLN02877 2.78e-75 77 574 197 802
alpha-amylase/limit dextrinase
TIGR02102 pullulan_Gpos 2.13e-74 91 606 310 912
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
CCV65359.1 8.45e-150 5 674 7 692
AIO18683.1 1.89e-142 2 674 4 699
CDR30743.1 1.09e-139 2 674 4 653
QMS84456.1 2.72e-135 5 674 7 699
ABX81149.1 5.14e-135 48 674 37 650

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3WDH_A 6.16e-115 5 622 13 650
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]
2E8Y_A 2.00e-110 73 604 79 631
Crystalstructure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Y_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 [Bacillus subtilis],2E8Z_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E8Z_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with alpha-cyclodextrin [Bacillus subtilis],2E9B_A Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis],2E9B_B Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose [Bacillus subtilis]
6JEQ_A 5.86e-108 58 614 5 586
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]
6JHH_A 8.84e-107 58 614 5 586
Crystalstructure of mutant D350A of Pullulanase from Paenibacillus barengoltzii complexed with maltotriose [Paenibacillus barengoltzii]
6JHI_A 8.84e-107 58 614 5 586
Crystalstructure of mutant D470A of Pullulanase from Paenibacillus barengoltzii complexed with maltotetraose [Paenibacillus barengoltzii]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
C0SPA0 7.81e-110 73 604 79 631
Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840 2.11e-80 100 637 225 801
Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
Q8GTR4 1.13e-54 69 574 177 795
Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2ZL64 1.07e-52 113 569 451 987
Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
A0A0H2UNG0 1.09e-52 113 569 466 1002
Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA 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
1.000046 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004538_00083.