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CAZyme Information: MGYG000001416_01682

You are here: Home > Sequence: MGYG000001416_01682

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 Cellulomonas massiliensis
Lineage Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Cellulomonadaceae; Cellulomonas; Cellulomonas massiliensis
CAZyme ID MGYG000001416_01682
CAZy Family GH13
CAZyme Description Glycogen debranching enzyme
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1924 MGYG000001416_1|CGC25 204124.63 4.4944
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001416 3245988 Isolate not provided not provided
Gene Location Start: 1799016;  End: 1804790  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 1323 1719 4.1e-160 0.997229916897507
GH13 215 564 1.3e-71 0.997229916897507

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
TIGR02103 pullul_strch 0.0 1039 1916 6 896
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 0.0 966 1916 31 968
alpha-amylase/limit dextrinase
cd11341 AmyAc_Pullulanase_LD-like 4.28e-168 1284 1746 1 391
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.
cd11339 AmyAc_bac_CMD_like_2 2.21e-134 163 624 1 344
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.
TIGR02104 pulA_typeI 8.26e-125 1164 1890 12 605
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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
AEE45261.1 0.0 9 1923 17 1948
VEH28739.1 0.0 9 1923 17 1948
AEI11455.1 0.0 1 1917 1 1912
QHT56497.1 0.0 45 1923 50 1947
QVI65018.1 0.0 1 1917 1 1911

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Y4S_A 3.57e-212 1037 1916 5 881
BarleyLimit Dextrinase In Complex With Beta-Cyclodextrin [Hordeum vulgare],2Y5E_A BARLEY LIMIT DEXTRINASE IN COMPLEX WITH ALPHA-CYCLODEXTRIN [Hordeum vulgare],4AIO_A Crystal structure of the starch debranching enzyme barley limit dextrinase [Hordeum vulgare],4CVW_A Structure of the barley limit dextrinase-limit dextrinase inhibitor complex [Hordeum vulgare],4CVW_B Structure of the barley limit dextrinase-limit dextrinase inhibitor complex [Hordeum vulgare]
4J3S_A 6.92e-212 1037 1916 26 902
Crystalstructure of barley limit dextrinase soaked with 300mM maltotetraose [Hordeum vulgare],4J3T_A Crystal structure of barley Limit dextrinase co-crystallized with 25mM maltotetraose [Hordeum vulgare],4J3U_A Crystal structure of barley limit dextrinase in complex with maltosyl-S-betacyclodextrin [Hordeum vulgare],4J3U_B Crystal structure of barley limit dextrinase in complex with maltosyl-S-betacyclodextrin [Hordeum vulgare],4J3V_A Crystal structure of barley limit dextrinase in complex with a branched thio-linked hexasaccharide [Hordeum vulgare]
4J3W_A 5.13e-211 1037 1916 26 902
Crystalstructure of barley limit dextrinase (E510A mutant) in complex with a branched maltohexasaccharide [Hordeum vulgare],4J3X_A Crystal structure of barley limit dextrinase (E510A mutant) in complex with a branched maltoheptasaccharide [Hordeum vulgare]
6J33_A 8.77e-188 1034 1914 143 1036
ChainA, pullulanase [Klebsiella pneumoniae],6J33_B Chain B, pullulanase [Klebsiella pneumoniae],6J34_A Chain A, Pullulanase [Klebsiella pneumoniae]
6J35_A 2.35e-186 1034 1914 143 1036
ChainA, Pullulanase [Klebsiella pneumoniae],6J35_B Chain B, Pullulanase [Klebsiella pneumoniae],6J4H_A Chain A, Pullulanase [Klebsiella pneumoniae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GTR4 1.42e-206 1039 1920 89 965
Pullulanase 1, chloroplastic OS=Arabidopsis thaliana OX=3702 GN=PU1 PE=1 SV=2
Q05884 1.33e-190 165 801 57 701
Alpha-amylase OS=Streptomyces lividans OX=1916 GN=amy PE=1 SV=1
P07206 3.61e-188 1034 1914 180 1073
Pullulanase OS=Klebsiella pneumoniae OX=573 GN=pulA PE=1 SV=2
P07811 4.65e-170 1034 1914 191 1083
Pullulanase OS=Klebsiella aerogenes OX=548 GN=pulA PE=1 SV=1
O33840 1.79e-57 1150 1867 215 801
Pullulanase OS=Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) OX=243274 GN=pulA PE=1 SV=2

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
0.001981 0.990955 0.000231 0.006295 0.000278 0.000232

TMHMM  Annotations      download full data without filtering help

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