Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30170.m014359 |
Family | GH13 |
Protein Properties | Length: 914 Molecular Weight: 103665 Isoelectric Point: 5.907 |
Chromosome | Chromosome/Scaffold: 30170 Start: 4111901 End: 4118689 |
Description | starch branching enzyme 2.2 |
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 | 335 | 660 | 1.5e-30 |
LPHIQANNYNTVQLMAVMEHSYYGSFGYHVTNFFAVSSRSGTPEDLKYLIDKAHSLGLRVLMDVVHSHASNNVTDGLNGFDVGQSSQDSYFHTADRGYHK LWDSRLFNYANWEVLRFLLSNLRWWLEEYKFDGFRFDGVTSMLYHHHGINMGFSGNYIEYFSEATDVDAVVYLMLANSLIHNLLPDATVIAEDVSGMPGL SCSVSEGGIGFDYRLAMAIPDKWIDYLKNKTDEEWSMGDISWSLTNRRYTEKCVAYAESHDQAIVGDKTIAFLLMDTEMYSGMSCLTDAPPTVERGIALH KMIHLLTMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 914 Download |
MTWRNNISYI SDLVTVGKHK RLQQSIIENK LGGREKSHEA EWLNLEKKML GSLTLFPAPV 60 FGSLANNSKR AFGNDCHITR QKPLGLIHRS QYLLGCPKVY FLSRFPVNKT VQHVLTASAV 120 MTDDSSTKTN IDEDMENIGL LSTDPGLDQF KDHFRYRVKR FIDQKQLIEK HEGGLEEFSK 180 GYQKFGFNRE DGSIVYREWA PAAQEAQVIG DFNGWNGSNH RMEKNEFGVW SIRIPDSAGN 240 PAIPHNSRVK FRFKHGNGAW VDRIPAWIRY ATVDPSSFGA PYDGVYWDPP ASERYQFKYP 300 RPPKPRAPRI YEAHVGMSSS EPRVNSYREF ADDVLPHIQA NNYNTVQLMA VMEHSYYGSF 360 GYHVTNFFAV SSRSGTPEDL KYLIDKAHSL GLRVLMDVVH SHASNNVTDG LNGFDVGQSS 420 QDSYFHTADR GYHKLWDSRL FNYANWEVLR FLLSNLRWWL EEYKFDGFRF DGVTSMLYHH 480 HGINMGFSGN YIEYFSEATD VDAVVYLMLA NSLIHNLLPD ATVIAEDVSG MPGLSCSVSE 540 GGIGFDYRLA MAIPDKWIDY LKNKTDEEWS MGDISWSLTN RRYTEKCVAY AESHDQAIVG 600 DKTIAFLLMD TEMYSGMSCL TDAPPTVERG IALHKMIHLL TMALGGEGYL NFMGNEFGHP 660 EWIDFPREGN GWSYDKCRRQ WNLVDTEHLR YKFMNAFDKA MNLLDEKHSF LSSTKQIVSS 720 TNEEDKAIVF ERGDLVFVFN FHPENTYDGY KVGCDLPGKY KVALDSDAWE FGGQGRVGHD 780 VDHFTSPEGI PGVPETNFNN RPNSFKVLSP PQTCVAYYRV QESQESNNSI NPGARNEIST 840 ADDVPKLRDI EVGMKQTLAA DTGAKRGDLE EVVNQTLASD AATMLEVFKE PADDKDTEEP 900 TVSVKKGNSK AQEI |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 3.0e-10 | 149 | 236 | 94 | + alpha-amylase | ||
PLN03244 | PLN03244 | 9.0e-136 | 241 | 780 | 545 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 103 | 846 | 744 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 292 | 699 | 408 | + Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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. | ||
PLN02960 | PLN02960 | 0 | 241 | 780 | 545 | + alpha-amylase |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
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 | ABN05321.1 | 0 | 63 | 857 | 17 | 811 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 49 | 883 | 1 | 835 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 49 | 851 | 1 | 810 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 73 | 851 | 7 | 787 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002510672.1 | 0 | 1 | 914 | 1 | 914 | starch branching enzyme II, 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 | 3aml_A | 0 | 129 | 860 | 2 | 728 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 129 | 825 | 2 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 129 | 825 | 2 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 129 | 825 | 2 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 0 | 199 | 822 | 32 | 617 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO619167 | 602 | 224 | 824 | 0 |
HO794536 | 712 | 140 | 838 | 0 |
HO777638 | 658 | 194 | 838 | 0 |
CX109187 | 404 | 437 | 840 | 0 |
HO777638 | 46 | 144 | 189 | 0.048 |
Sequence Alignments (This image is cropped. Click for full image.) |
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