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CAZyme Information: MGYG000004028_00885

You are here: Home > Sequence: MGYG000004028_00885

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
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Oscillospiraceae; CAG-83;
CAZyme ID MGYG000004028_00885
CAZy Family GH13
CAZyme Description Amylopullulanase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
624 MGYG000004028_21|CGC1 70738.41 4.9571
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004028 2349956 MAG United Kingdom Europe
Gene Location Start: 6174;  End: 8048  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004028_00885.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH13 186 515 8.7e-130 0.9936708860759493

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
cd11338 AmyAc_CMD 0.0 132 552 1 389
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 7.02e-125 125 589 114 567
maltodextrin glucosidase; Provisional
PRK14510 PRK14510 2.24e-97 17 571 6 599
bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase.
COG0366 AmyA 2.32e-61 133 531 1 380
Glycosidase [Carbohydrate transport and metabolism].
cd11316 AmyAc_bac2_AmyA 2.15e-60 186 550 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
BCK82421.1 5.70e-293 16 624 5 613
QUO34762.1 3.90e-282 9 624 3 616
BCK79563.1 1.19e-259 16 624 5 607
QNL44205.1 1.08e-250 16 624 5 617
QCI59536.1 1.05e-249 15 617 6 615

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5BN7_A 7.61e-78 127 586 119 568
Crystalstructure of maltodextrin glucosidase from E.coli at 3.7 A resolution [Escherichia coli K-12]
2WC7_A 1.01e-76 126 580 5 434
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 4.44e-75 127 622 129 582
CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501]
2Z1K_A 5.69e-75 128 566 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]
5OT1_A 1.09e-74 73 566 236 709
ChainA, Pullulanase type II, GH13 family [Thermococcus kodakarensis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P38939 1.03e-112 17 624 256 918
Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2
P16950 3.18e-110 17 624 256 919
Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1
P36905 1.24e-105 17 624 259 921
Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2
P38536 5.65e-102 17 624 259 920
Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2
P21517 3.18e-77 127 586 117 566
Maltodextrin glucosidase OS=Escherichia coli (strain K12) OX=83333 GN=malZ PE=1 SV=5

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
0.986701 0.013132 0.000076 0.000051 0.000020 0.000049

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004028_00885.