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CAZyme Information: MGYG000001354_00775

You are here: Home > Sequence: MGYG000001354_00775

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 Bifidobacterium dentium
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Bifidobacteriaceae; Bifidobacterium; Bifidobacterium dentium
CAZyme ID MGYG000001354_00775
CAZy Family GH13
CAZyme Description Pullulanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
682 MGYG000001354_1|CGC17 75814.02 5.0834
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001354 2642081 Isolate not provided not provided
Gene Location Start: 916957;  End: 919005  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001354_00775.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 193 547 4.4e-102 0.9930795847750865

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11341 AmyAc_Pullulanase_LD-like 0.0 147 590 4 406
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.
TIGR02104 pulA_typeI 0.0 23 661 9 605
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.
COG1523 PulA 6.35e-116 16 602 16 602
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
TIGR02103 pullul_strch 4.39e-90 26 570 128 728
alpha-1,6-glucosidases, pullulanase-type. Members of this protein family include secreted (or membrane-anchored) pullulanases of Gram-negative bacteria and pullulanase-type starch debranching enzymes of plants. Both enzymes hydrolyze alpha-1,6 glycosidic linkages. 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 is closely homologous to, but architecturally different from, the Gram-positive pullulanases of Gram-positive bacteria (TIGR02102). [Energy metabolism, Biosynthesis and degradation of polysaccharides]
PLN02877 PLN02877 4.34e-79 26 570 215 797
alpha-amylase/limit dextrinase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
VEG24732.1 0.0 1 682 1 682
ADB10752.1 0.0 1 682 1 682
BAQ28058.1 0.0 1 682 1 682
QTL77805.1 0.0 1 682 1 682
QTL79660.1 0.0 1 682 1 682

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7LSA_A 4.07e-138 26 590 64 611
ChainA, Pullulanase [Ruminococcus bromii]
7LSR_A 6.27e-137 26 590 64 611
ChainA, Pullulanase [Ruminococcus bromii]
7LSU_A 6.61e-137 26 590 64 611
ChainA, Pullulanase [Ruminococcus bromii]
7LST_A 6.79e-137 26 590 64 611
ChainA, Pullulanase [Ruminococcus bromii]
6JEQ_A 2.13e-127 26 594 41 562
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
C0SPA0 4.98e-99 25 594 105 617
Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1
O33840 7.72e-99 25 594 224 749
Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
Q8GTR4 2.84e-55 26 573 208 793
Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
A0A0H2UNG0 3.17e-51 25 633 450 1091
Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
P07206 4.64e-51 27 618 305 955
Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA 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
1.000046 0.000015 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001354_00775.