Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30170.m013877 |
Family | GH13 |
Protein Properties | Length: 422 Molecular Weight: 47295.4 Isoelectric Point: 5.2627 |
Chromosome | Chromosome/Scaffold: 30170 Start: 1513636 End: 1515349 |
Description | alpha-amylase-like |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 29 | 339 | 9.80909e-45 |
ESCNKEGGWYNSLKNFVPDIASAGITHVWLPPSSQSVAPQGYMPGRLYDLSVSKYGNQDELKSLIQALHQKGIKCLADIVINHRTAEKQDERGIWCIFEG GTADDRLDWGPSFICRDDTAYSDGKGNPDTGGDFEPAPDIDHLNPRVQQELSDWMNWLKSEIGFDGWRFDYVKGYAPSITKIYMGKTTPDFAVGEKWDSL SYGQDRKPDYNQDGHRNALKDWIQAAGGVITAFDFTTKGILQAAVQGELWRLKDSNGNPPGLIGTMPQNAVTFIDNHDTGSTQQLWPFPSDKVMQGYAYI LTHPGIPSIFY |
Full Sequence |
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Protein Sequence Length: 422 Download |
MTFLSWFYLL SIFPLYTSAA VLFQGFNWES CNKEGGWYNS LKNFVPDIAS AGITHVWLPP 60 SSQSVAPQGY MPGRLYDLSV SKYGNQDELK SLIQALHQKG IKCLADIVIN HRTAEKQDER 120 GIWCIFEGGT ADDRLDWGPS FICRDDTAYS DGKGNPDTGG DFEPAPDIDH LNPRVQQELS 180 DWMNWLKSEI GFDGWRFDYV KGYAPSITKI YMGKTTPDFA VGEKWDSLSY GQDRKPDYNQ 240 DGHRNALKDW IQAAGGVITA FDFTTKGILQ AAVQGELWRL KDSNGNPPGL IGTMPQNAVT 300 FIDNHDTGST QQLWPFPSDK VMQGYAYILT HPGIPSIFYD HFFDWGLKEP ISRLASIRKS 360 YGIDSKSRVK IVAAESDLYM AAINDNVIMK IGPKMDLGNL LPSKEFQVAT SGESYAVWVK 420 KV |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 2.0e-52 | 21 | 361 | 412 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02784 | PLN02784 | 4.0e-144 | 21 | 421 | 405 | + alpha-amylase | ||
PLN02361 | PLN02361 | 6.0e-150 | 21 | 420 | 404 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 8.0e-163 | 21 | 369 | 352 | + 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 | 1 | 420 | 423 | + alpha-amylase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004556 | alpha-amylase activity |
GO:0005509 | calcium ion binding |
GO:0005975 | carbohydrate metabolic process |
GO:0043169 | cation binding |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PRF/SEQDB | 0 | 4 | 418 | 7 | 420 | UP10_LACSN Unknown protein 10 from 2D-PAGE | |
RefSeq | XP_002301187.1 | 0 | 20 | 421 | 4 | 404 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002327139.1 | 0 | 1 | 420 | 4 | 423 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510218.1 | 0 | 1 | 422 | 1 | 422 | alpha-amylase, putative [Ricinus communis] |
RefSeq | XP_002510219.1 | 0 | 23 | 420 | 29 | 426 | pentatricopeptide repeat-containing protein, putative [Ricinus communis] |
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 | 1bg9_A | 0 | 21 | 420 | 2 | 402 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 Complexed With Udp-Glucose |
PDB | 1ava_B | 0 | 21 | 420 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 21 | 420 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 21 | 420 | 2 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qpu_C | 0 | 21 | 420 | 3 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |