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CAZyme Information: MGYG000002403_04842

You are here: Home > Sequence: MGYG000002403_04842

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 Robinsoniella peoriensis
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella peoriensis
CAZyme ID MGYG000002403_04842
CAZy Family GH13
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
662 MGYG000002403_126|CGC1 73784.68 4.4138
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002403 7202103 Isolate not provided not provided
Gene Location Start: 14552;  End: 16540  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.1 2.4.1.-

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 79 410 6.5e-59 0.9673202614379085
CBM20 569 655 9.3e-26 0.9444444444444444

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11320 AmyAc_AmyMalt_CGTase_like 1.88e-123 38 462 3 387
Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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 3.47e-74 38 465 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.
cd11319 AmyAc_euk_AmyA 1.11e-67 38 463 7 370
Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. 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.
cd11340 AmyAc_bac_CMD_like_3 8.28e-49 42 408 6 352
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.
pfam00128 Alpha-amylase 1.94e-48 80 415 1 332
Alpha amylase, catalytic domain. Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCN31337.1 0.0 10 662 8 661
BBF44647.1 0.0 10 662 3 662
AQR97595.1 2.78e-235 29 581 31 585
AGF58924.1 1.12e-234 29 581 31 585
BAF37283.1 2.68e-210 28 580 30 578

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1A47_A 2.06e-77 40 662 15 681
CGTASEFROM THERMOANAEROBACTERIUM THERMOSULFURIGENES EM1 IN COMPLEX WITH A MALTOHEXAOSE INHIBITOR [Thermoanaerobacterium thermosulfurigenes],1CIU_A Thermostable Cgtase From Thermoanaerobacterium Thermosulfurigenes Em1 At Ph 8.0. [Thermoanaerobacterium thermosulfurigenes]
1CYG_A 3.75e-77 40 662 12 678
CyclodextrinGlucanotransferase (E.C.2.4.1.19) (Cgtase) [Geobacillus stearothermophilus]
3BMV_A 5.55e-77 40 662 15 681
ChainA, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes],3BMW_A Chain A, Cyclomaltodextrin glucanotransferase [Thermoanaerobacterium thermosulfurigenes]
1I75_A 2.06e-67 40 662 15 684
CRYSTALSTRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1I75_B CRYSTAL STRUCTURE OF CYCLODEXTRIN GLUCANOTRANSFERASE FROM ALKALOPHILIC BACILLUS SP.#1011 COMPLEXED WITH 1-DEOXYNOJIRIMYCIN [Bacillus sp. (in: Bacteria)],1PAM_A CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1PAM_B CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1UKQ_A Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011],1UKQ_B Crystal structure of cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose [Bacillus sp. 1011]
1D7F_A 2.06e-67 40 662 15 684
ChainA, CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1D7F_B Chain B, CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1DED_A Chain A, CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011],1DED_B Chain B, CYCLODEXTRIN GLUCANOTRANSFERASE [Bacillus sp. 1011]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P26827 7.21e-77 19 662 10 708
Cyclomaltodextrin glucanotransferase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyA PE=1 SV=2
P31797 1.02e-76 24 662 27 709
Cyclomaltodextrin glucanotransferase OS=Geobacillus stearothermophilus OX=1422 GN=cgt PE=1 SV=1
P21543 4.94e-69 40 558 747 1194
Beta/alpha-amylase OS=Paenibacillus polymyxa OX=1406 PE=1 SV=1
P09121 2.60e-68 28 662 24 710
Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 38-2) OX=1412 GN=cgt PE=1 SV=2
P05618 2.57e-67 28 662 24 711
Cyclomaltodextrin glucanotransferase OS=Bacillus sp. (strain 1011) OX=1410 GN=cgt 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
0.000340 0.998857 0.000220 0.000205 0.000188 0.000165

TMHMM  Annotations      download full data without filtering help

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12 34