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CAZyme Information: MGYG000001371_01993

You are here: Home > Sequence: MGYG000001371_01993

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 Paenibacillus lautus_A
Lineage Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lautus_A
CAZyme ID MGYG000001371_01993
CAZy Family CBM41
CAZyme Description Glycogen debranching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2530 MGYG000001371_46|CGC2 275768.33 4.624
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001371 6950059 Isolate not provided not provided
Gene Location Start: 43033;  End: 50625  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.41 3.2.1.1

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 1684 1994 2.8e-121 0.9965986394557823
GH13 734 1072 5.3e-111 0.9964788732394366
CBM41 365 470 7.7e-29 0.9803921568627451
CBM41 254 355 2.4e-27 0.9607843137254902

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02102 pullulan_Gpos 0.0 251 1247 1 1003
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 (.
cd11341 AmyAc_Pullulanase_LD-like 6.83e-145 706 1141 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.
TIGR02104 pulA_typeI 2.58e-144 562 1222 3 605
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 1.95e-139 499 1195 1 635
Pullulanase/glycogen debranching enzyme [Carbohydrate transport and metabolism].
cd11339 AmyAc_bac_CMD_like_2 7.70e-79 1653 2035 4 344
Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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
ACX62652.1 0.0 1 2530 1 2528
AYB46879.1 0.0 1 2530 1 2527
QOT09076.1 0.0 1 2530 1 2527
QCT01087.1 0.0 5 2530 5 2525
QMV42545.1 0.0 1 2528 1 2511

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2YA1_A 2.63e-270 254 1247 7 1010
Productcomplex of a multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
2YA2_A 1.08e-214 556 1247 1 704
CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA in complex with an inhibitor. [Streptococcus pneumoniae TIGR4]
2YA0_A 1.33e-214 558 1247 2 703
CatalyticModule of the Multi-modular glycogen-degrading pneumococcal virulence factor SpuA [Streptococcus pneumoniae TIGR4]
3FAW_A 2.12e-213 447 1247 10 812
CrystalStructure of the Group B Streptococcus Pullulanase SAP [Streptococcus agalactiae COH1],3FAX_A The crystal structure of GBS pullulanase SAP in complex with maltotetraose [Streptococcus agalactiae COH1]
2WAN_A 1.14e-79 258 1219 9 898
Pullulanasefrom Bacillus acidopullulyticus [Bacillus acidopullulyticus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
A0A0H2UNG0 8.53e-267 250 1247 132 1139
Pullulanase A OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=spuA PE=1 SV=1
Q9F930 1.05e-266 206 1247 98 1146
Pullulanase A OS=Streptococcus pneumoniae OX=1313 GN=spuA PE=1 SV=1
A0A0H2ZL64 1.12e-266 250 1247 117 1124
Pullulanase A OS=Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) OX=373153 GN=spuA PE=3 SV=1
O33840 1.10e-76 365 1246 22 840
Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2
C0SPA0 1.41e-66 562 1166 97 638
Pullulanase OS=Bacillus subtilis (strain 168) OX=224308 GN=amyX PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000281 0.999036 0.000168 0.000191 0.000156 0.000140

TMHMM  Annotations      download full data without filtering help

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12 31