Species | UMGS1688 sp900754695 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; CAG-917; UMGS1688; UMGS1688 sp900754695 | |||||||||||
CAZyme ID | MGYG000002009_00338 | |||||||||||
CAZy Family | GH13 | |||||||||||
CAZyme Description | Amylopullulanase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 28617; End: 30425 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GH13 | 174 | 502 | 4.1e-117 | 0.9936708860759493 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd11338 | AmyAc_CMD | 1.48e-158 | 124 | 536 | 1 | 385 | 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 | 3.08e-81 | 116 | 558 | 113 | 551 | maltodextrin glucosidase; Provisional |
PRK14510 | PRK14510 | 9.67e-67 | 28 | 529 | 15 | 567 | bifunctional glycogen debranching protein GlgX/4-alpha-glucanotransferase. |
COG0366 | AmyA | 9.01e-43 | 125 | 522 | 1 | 382 | Glycosidase [Carbohydrate transport and metabolism]. |
pfam00128 | Alpha-amylase | 5.14e-42 | 174 | 502 | 1 | 334 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QNK39367.1 | 3.30e-157 | 9 | 600 | 10 | 613 |
CAB1243760.1 | 8.16e-155 | 6 | 581 | 7 | 579 |
QAT48387.1 | 1.04e-154 | 9 | 539 | 10 | 546 |
QCX33355.1 | 2.67e-154 | 9 | 566 | 15 | 585 |
CAB1239245.1 | 3.23e-153 | 4 | 555 | 6 | 563 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
1SMA_A | 4.51e-66 | 116 | 594 | 126 | 577 | CrystalStructure Of A Maltogenic Amylase [Thermus sp. IM6501],1SMA_B Crystal Structure Of A Maltogenic Amylase [Thermus sp. IM6501] |
1J0H_A | 8.72e-66 | 116 | 594 | 126 | 577 | Crystalstructure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0H_B Crystal structure of Bacillus stearothermophilus neopullulanase [Geobacillus stearothermophilus],1J0I_A Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus],1J0I_B Crystal structure of neopullulanase complex with panose [Geobacillus stearothermophilus] |
1J0J_A | 2.35e-65 | 116 | 594 | 126 | 577 | ChainA, neopullulanase [Geobacillus stearothermophilus],1J0J_B Chain B, neopullulanase [Geobacillus stearothermophilus],1J0K_A Chain A, neopullulanase [Geobacillus stearothermophilus],1J0K_B Chain B, neopullulanase [Geobacillus stearothermophilus] |
1GVI_A | 6.30e-65 | 116 | 594 | 126 | 577 | Thermusmaltogenic amylase in complex with beta-CD [Thermus sp.],1GVI_B Thermus maltogenic amylase in complex with beta-CD [Thermus sp.] |
1JF6_A | 1.15e-64 | 85 | 540 | 91 | 506 | ChainA, ALPHA AMYLASE II [Thermoactinomyces vulgaris],1JF6_B Chain B, ALPHA AMYLASE II [Thermoactinomyces vulgaris] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P38939 | 6.48e-92 | 1 | 565 | 248 | 858 | Amylopullulanase OS=Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E) OX=340099 GN=apu PE=1 SV=2 |
P16950 | 6.80e-90 | 1 | 581 | 248 | 873 | Amylopullulanase OS=Thermoanaerobacter thermohydrosulfuricus OX=1516 GN=apu PE=1 SV=1 |
P36905 | 1.05e-89 | 1 | 565 | 251 | 859 | Amylopullulanase OS=Thermoanaerobacterium saccharolyticum OX=28896 GN=apu PE=3 SV=2 |
P38536 | 2.24e-87 | 1 | 565 | 251 | 858 | Amylopullulanase OS=Thermoanaerobacterium thermosulfurigenes OX=33950 GN=amyB PE=3 SV=2 |
Q08341 | 9.53e-68 | 119 | 558 | 128 | 529 | Cyclomaltodextrinase OS=Lysinibacillus sphaericus OX=1421 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000064 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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