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CAZyme Information: MGYG000002882_01398

You are here: Home > Sequence: MGYG000002882_01398

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-83 sp000435975
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-83; CAG-83 sp000435975
CAZyme ID MGYG000002882_01398
CAZy Family GH13
CAZyme Description Amylopullulanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
612 69603.81 5.1451
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002882 2163775 MAG United States North America
Gene Location Start: 29946;  End: 31784  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002882_01398.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 174 503 6.7e-129 0.9936708860759493

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11338 AmyAc_CMD 0.0 121 540 2 389
Alpha amylase catalytic domain found in 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). 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.
PRK10785 PRK10785 1.78e-115 40 604 35 597
maltodextrin glucosidase; Provisional
PRK14510 PRK14510 5.99e-98 1 539 1 576
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
COG0366 AmyA 3.56e-62 121 589 1 505
Glycosidase [Carbohydrate transport and metabolism].
cd11316 AmyAc_bac2_AmyA 4.97e-58 174 538 20 403
Alpha amylase catalytic domain found in bacterial 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 Chloroflexi, Dictyoglomi, and Fusobacteria. 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
QUO34762.1 0.0 1 612 5 616
BCK82421.1 0.0 1 612 1 613
BCK79563.1 1.89e-284 1 612 1 607
QNL44205.1 2.72e-272 1 612 1 617
BAL01834.1 2.78e-271 4 612 16 633

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2Z1K_A 4.54e-74 116 554 2 413
CrystalStructure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_B Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_C Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8],2Z1K_D Crystal Structure of Ttha1563 from Thermus thermophilus HB8 [Thermus thermophilus HB8]
2WC7_A 6.35e-74 115 576 6 442
Crystalstructure of Nostoc Punctiforme Debranching Enzyme(NPDE)(Acarbose soaked) [Nostoc punctiforme],2WCS_A Crystal Structure of Debranching enzyme from Nostoc punctiforme (NPDE) [Nostoc punctiforme],2WKG_A Chain A, Alpha Amylase, Catalytic Region [Nostoc punctiforme PCC 73102]
1SMA_A 3.75e-71 114 605 128 577
CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
5OT1_A 7.78e-71 5 587 188 748
ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]
5BN7_A 9.51e-71 41 577 37 570
Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P36905 1.37e-113 6 612 259 921
Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38939 1.70e-105 6 612 256 918
Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950 4.22e-105 6 612 256 919
Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P38536 6.19e-105 6 612 259 920
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
A0A7U9P668 2.05e-70 114 605 128 577
Cyclomaltodextrinase OS=Geobacillus thermopakistaniensis (strain MAS1) OX=1408282 GN=T260_08735 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
1.000008 0.000019 0.000003 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002882_01398.