Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 29736.m002033 |
Family | CBM45 |
Protein Properties | Length: 900 Molecular Weight: 101199 Isoelectric Point: 5.9776 |
Chromosome | Chromosome/Scaffold: 29736 Start: 227328 End: 236463 |
Description | alpha-amylase-like 3 |
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 |
CBM45 | 313 | 389 | 7.4e-25 |
LHWGVCRDDAKNWEIPSSPHPPETTVFKNKALQTMLQPNDGGNGCSGLFSLDEEFAGFLFVLKLNEGTWLKCKGNDF | |||
CBM45 | 124 | 207 | 2.9e-28 |
LHWGVSYVGDVGSEWDQPPKNMRPRGSISIKDYAIETPLEKSSEADMFYEVKIDLDPNSSIAAINFVLKDEETGAWYQHKGRDF | |||
GH13 | 533 | 821 | 2.2e-38 |
KAAEISSLGFTVIWLPPPTESVSPEGYMPKDLYNLNSRYGSIDELKDLVKSLHRVGLKVLGDAVLNHRCAHFQNQNGVWNIFGGRLNWDDRAIVADDPHF QGRGSKSSGDNFHAAPNIDHSQDFVRQDLKEWLCWLRDEIGYNGWRLDFVRGFWGGYVKDYMEATEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIIDWI NATNGTAGAFDVTTKGILHSALDRCEYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPNGKEMQGYAYILTHPGTPTVFY |
Full Sequence |
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Protein Sequence Length: 900 Download |
MSTLTVEPLL RFSGREKSLP IGSRKILKPS SLNFSKKLLL SNGSSFCNFK RSPPLSHTVR 60 ASSTTDTALI ETFKSADVLF KETFSLSRTE TIEGKIFVRL DKEEKDQQRW QLSVGCSLPG 120 KWILHWGVSY VGDVGSEWDQ PPKNMRPRGS ISIKDYAIET PLEKSSEADM FYEVKIDLDP 180 NSSIAAINFV LKDEETGAWY QHKGRDFKVP LVDYLLEGGN VVGAKRGFSI WPGSLLSNML 240 LKTETLPSKD EDNNSETKDV KQDSGQLKGF YEEQPITKQV TIQNSATVSV TKCPKTAKYL 300 LYLETDLPGE VVLHWGVCRD DAKNWEIPSS PHPPETTVFK NKALQTMLQP NDGGNGCSGL 360 FSLDEEFAGF LFVLKLNEGT WLKCKGNDFY VPLSTSSSLP TQPGQGQSEG VLASGKDAEG 420 NEEVSRTAYT DEIIDEIRNL VNGISSEKVR QTKTKEAQES ILQEIEKLAA EAYSIFRSSI 480 PTFTEESVLE SEVEKAPPAK ICSGTGTGHE ILLQGFNWES NKSGRWHMEL KEKAAEISSL 540 GFTVIWLPPP TESVSPEGYM PKDLYNLNSR YGSIDELKDL VKSLHRVGLK VLGDAVLNHR 600 CAHFQNQNGV WNIFGGRLNW DDRAIVADDP HFQGRGSKSS GDNFHAAPNI DHSQDFVRQD 660 LKEWLCWLRD EIGYNGWRLD FVRGFWGGYV KDYMEATEPY FAVGEYWDSL SYTYGEMDHN 720 QDAHRQRIID WINATNGTAG AFDVTTKGIL HSALDRCEYW RLSDQKGKPP GVVGWWPSRA 780 VTFIENHDTG STQGHWRFPN GKEMQGYAYI LTHPGTPTVF YDHIFSHYRS EIASLISLRK 840 RNEIHCRSSV KITKAERDVY AAIIEEKVAM KIGPGHYEPP SGKNWSMAIE GKDYKVWEAS 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 2.0e-49 | 507 | 841 | 415 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 2.0e-133 | 510 | 898 | 406 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-165 | 511 | 850 | 343 | + 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. | ||
PLN02361 | PLN02361 | 1.0e-170 | 508 | 898 | 397 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 900 | 903 | + alpha-amylase |
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 |
GenBank | AAX33231.1 | 0 | 1 | 900 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
EMBL | CAN69906.1 | 0 | 1 | 900 | 1 | 887 | hypothetical protein [Vitis vinifera] |
EMBL | CBI32016.1 | 0 | 1 | 900 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 900 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 900 | 1 | 900 | alpha-amylase, 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 | 2qpu_C | 0 | 509 | 898 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 509 | 898 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 509 | 898 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 509 | 898 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 509 | 898 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 910 | 1 | 900 | 0 |
HO826981 | 405 | 497 | 900 | 0 |
EG663543 | 290 | 496 | 785 | 0 |
ES805448 | 329 | 466 | 794 | 0 |
HO826981 | 27 | 464 | 490 | 0.013 |
Sequence Alignments (This image is cropped. Click for full image.) |
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