Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_30833g0020 |
Family | GH13 |
Protein Properties | Length: 462 Molecular Weight: 51269.9 Isoelectric Point: 5.4443 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 63 | 374 | 1.6e-37 |
LKGIVKDAADAGITDVWFPPPSQSLAPEGYLPQRLYDLKSSKYGSEQELRDAVNAFHQKGIGCVGDIVINHRCGTKQDDKGMWCVFEGGKGDGRLDWGPW AVTVNDLDWGPWAVCVNDKPYPCGSGHADTGDDYTAAPDIDHTNPAIQADLSEWMNWLKSHVGFDGWRFDFAKGYAGNLLGIYVENTNPKFVVGEVWDDM AYGSDGRLVYDQDAHRQKLVNWVHSTGDRASAFDFTTKGILQEAVEANELWRLRDSNGRPTGMIGFWPQKAVTFIDNHDTGSTQKMWPFPSDKLLQGYAY ILTHPGIPTIFY |
Full Sequence |
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Protein Sequence Length: 462 Download |
MAKFGLLSLL LCSCIVIIAA SPAQARTAST VSKLSKTDPL NTVLLQGFNW ESAKSSSSWY 60 NVLKGIVKDA ADAGITDVWF PPPSQSLAPE GYLPQRLYDL KSSKYGSEQE LRDAVNAFHQ 120 KGIGCVGDIV INHRCGTKQD DKGMWCVFEG GKGDGRLDWG PWAVTVNDLD WGPWAVCVND 180 KPYPCGSGHA DTGDDYTAAP DIDHTNPAIQ ADLSEWMNWL KSHVGFDGWR FDFAKGYAGN 240 LLGIYVENTN PKFVVGEVWD DMAYGSDGRL VYDQDAHRQK LVNWVHSTGD RASAFDFTTK 300 GILQEAVEAN ELWRLRDSNG RPTGMIGFWP QKAVTFIDNH DTGSTQKMWP FPSDKLLQGY 360 AYILTHPGIP TIFYDHFVDG NMKKEIQTLI AIRKRNNINA SSNCRIIIAD GDLYMAAIDE 420 KIVMKIGSRY DVGKLAPPSP EFRIVASGND YCVWEKNSFP VE |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 2.0e-28 | 195 | 412 | 242 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02784 | PLN02784 | 3.0e-143 | 43 | 456 | 416 | + alpha-amylase | ||
PLN02361 | PLN02361 | 8.0e-153 | 43 | 456 | 417 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-158 | 43 | 403 | 363 | + Alpha amylase catalytic domain found in archaeal, bacterial, and plant 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 AmyA from bacteria, archaea, water fleas, and plants. 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. | ||
PLN00196 | PLN00196 | 0 | 34 | 457 | 427 | + alpha-amylase; Provisional |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABK24287.1 | 0 | 1 | 458 | 1 | 447 | unknown [Picea sitchensis] |
GenBank | ABK24434.1 | 0 | 1 | 460 | 1 | 447 | unknown [Picea sitchensis] |
GenBank | ABR16554.1 | 0 | 1 | 458 | 1 | 447 | unknown [Picea sitchensis] |
DDBJ | BAC02435.1 | 0 | 1 | 456 | 1 | 422 | alpha-amylase [Ipomoea nil] |
RefSeq | XP_002301187.1 | 0 | 42 | 456 | 4 | 403 | predicted protein [Populus trichocarpa] |
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 | 3bsg_A | 0 | 41 | 457 | 1 | 405 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 41 | 457 | 1 | 405 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1p6w_A | 0 | 41 | 457 | 1 | 405 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1ht6_A | 0 | 41 | 457 | 1 | 405 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
PDB | 2qpu_C | 0 | 41 | 457 | 1 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |