Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_159157g0180 |
Family | GH13 |
Protein Properties | Length: 543 Molecular Weight: 61314.6 Isoelectric Point: 4.8291 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 46 | 383 | 0 |
GDLRGVIERLPYLRELGVDALWLSPIFPSPMEDFGYDISDYTGIDPLFGTLADFDALVAAAHDFGLKIILDLVPNHTSDQHPWFIESRGSRDSAKRDWYI WRDPKGEGGPPNNWLSEFGGSTWEFDAHTGQYYYHAFLRSQPDLNWRNPEVRGAMHDVMRFWLRRGVDGFRVDVMWHLIKDDLLRDNPPNPDFVPGQQPY EQLIPLYSTDRPEVHDVVAELRQVIDEFEDRVLIGEIYLPPAKLAAYYGRDLAGAHLPFNFALISTPWNARAIAKLVDDYEAALPAGAWPNWVLGNHDRQ RIASRLGTDQARVAAMLLLTLRGTPTLYYGDEIGMPQV |
Full Sequence |
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Protein Sequence Length: 543 Download |
MCRFSIVFTV TGLACAMREN VPWWKSGILY QIYPRSFQDS DGDGLGDLRG VIERLPYLRE 60 LGVDALWLSP IFPSPMEDFG YDISDYTGID PLFGTLADFD ALVAAAHDFG LKIILDLVPN 120 HTSDQHPWFI ESRGSRDSAK RDWYIWRDPK GEGGPPNNWL SEFGGSTWEF DAHTGQYYYH 180 AFLRSQPDLN WRNPEVRGAM HDVMRFWLRR GVDGFRVDVM WHLIKDDLLR DNPPNPDFVP 240 GQQPYEQLIP LYSTDRPEVH DVVAELRQVI DEFEDRVLIG EIYLPPAKLA AYYGRDLAGA 300 HLPFNFALIS TPWNARAIAK LVDDYEAALP AGAWPNWVLG NHDRQRIASR LGTDQARVAA 360 MLLLTLRGTP TLYYGDEIGM PQVAIAPDRV RDPWEKNVPG MGVGRDGCRT PMQWDDTAYA 420 GFSVREPWLP LSKDIALVNV ATERQDTASM LSLYRALVTL RRARPELALG GYRLVSVADE 480 LLVYAREHQD QRSLIALNLG MATVSLEVRG HVLLSTFMDR QAEVIDGLLS LRGAEGIVIE 540 PSS |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd11331 | AmyAc_OligoGlu_like | 0 | 22 | 471 | 450 | + Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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. | ||
cd11333 | AmyAc_SI_OligoGlu_DGase | 0 | 25 | 462 | 456 | + Alpha amylase catalytic domain found in Sucrose isomerases, oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase), dextran glucosidase (also called glucan 1,6-alpha-glucosidase), and related proteins. The sucrose isomerases (SIs) Isomaltulose synthase (EC 5.4.99.11) and Trehalose synthase (EC 5.4.99.16) catalyze the isomerization of sucrose and maltose to produce isomaltulose and trehalulose, respectively. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomaltooligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. Dextran glucosidase (DGase, EC 3.2.1.70) hydrolyzes alpha-1,6-glucosidic linkages at the non-reducing end of panose, isomaltooligosaccharides and dextran to produce alpha-glucose.The common reaction chemistry of the alpha-amylase family enzymes is based on a two-step acid catalytic mechanism that requires two critical carboxylates: one acting as a general acid/base (Glu) and the other as a nucleophile (Asp). Both hydrolysis and transglycosylation proceed via the nucleophilic substitution reaction between the anomeric carbon, C1 and a nucleophile. Both enzymes contain the three catalytic residues (Asp, Glu and Asp) common to the alpha-amylase family as well as two histidine residues which are predicted to be critical to binding the glucose residue adjacent to the scissile bond in the substrates. 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 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. | ||
cd11359 | AmyAc_SLC3A1 | 0 | 22 | 461 | 453 | + Alpha amylase catalytic domain found in Solute Carrier family 3 member 1 proteins. SLC3A1, also called Neutral and basic amino acid transport protein rBAT or NBAT, plays a role in amino acid and cystine absorption. Mutations in the gene encoding SLC3A1 causes cystinuria, an autosomal recessive disorder characterized by the failure of proximal tubules to reabsorb filtered cystine and dibasic amino acids. 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. | ||
cd11328 | AmyAc_maltase | 0 | 23 | 472 | 468 | + Alpha amylase catalytic domain found in maltase (also known as alpha glucosidase) and related proteins. Maltase (EC 3.2.1.20) hydrolyzes the terminal, non-reducing (1->4)-linked alpha-D-glucose residues in maltose, releasing alpha-D-glucose. In most cases, maltase is equivalent to alpha-glucosidase, but the term "maltase" emphasizes the disaccharide nature of the substrate from which glucose is cleaved, and the term "alpha-glucosidase" emphasizes the bond, whether the substrate is a disaccharide or polysaccharide. 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. | ||
cd11330 | AmyAc_OligoGlu | 0 | 22 | 482 | 473 | + Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | NP_950093.1 | 0 | 20 | 539 | 6 | 530 | glycosy hydrolase family protein [Rhodopseudomonas palustris CGA009] |
RefSeq | YP_001202693.1 | 0 | 17 | 539 | 1 | 528 | alpha-glucosidase [Bradyrhizobium sp. ORS278] |
RefSeq | YP_001994205.1 | 0 | 20 | 539 | 6 | 530 | alpha amylase catalytic region [Rhodopseudomonas palustris TIE-1] |
RefSeq | YP_534732.1 | 0 | 23 | 542 | 9 | 533 | alpha amylase, catalytic region [Rhodopseudomonas palustris BisB18] |
RefSeq | YP_783764.1 | 0 | 20 | 542 | 6 | 533 | alpha amylase, catalytic region [Rhodopseudomonas palustris BisA53] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2ze0_A | 0 | 23 | 499 | 5 | 506 | A Chain A, Alpha-glucosidase Gsj |
PDB | 1uok_A | 0 | 23 | 508 | 5 | 519 | A Chain A, Crystal Structure Of B. Cereus Oligo-1,6-Glucosidase |
PDB | 4gin_A | 0 | 1 | 499 | 12 | 536 | A Chain A, Crystal Structure Of The Mutb R284c Mutant From Crystals Soaked With The Inhibitor Deoxynojirimycin |
PDB | 4aie_A | 0 | 23 | 521 | 6 | 522 | A Chain A, Structure Of Glucan-1,6-Alpha-Glucosidase From Lactobacillus Acidophilus Ncfm |
PDB | 4h2c_A | 0 | 21 | 499 | 4 | 509 | A Chain A, Trehalulose Synthase Mutb R284c Mutant |