y
Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 27496.m000095 |
Family | GH13 |
Protein Properties | Length: 863 Molecular Weight: 98719.1 Isoelectric Point: 5.0181 |
Chromosome | Chromosome/Scaffold: 27496 Start: 6548 End: 21801 |
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 | 353 | 672 | 1.1e-27 |
LPRIKRLGYNTVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPDDLKSLIDKAHELDLLVLMDIVHSHSSNNTLDGLNMFDGTDGHYFHSGSRGYHWMWD SRLFNYGSWEVLRFLLSNARWWLDEYKFDGFRFDGVTSMMYTHHGLEVAFTGNYNEYFGFATDVDAVVYLMLVNDMIHGLFPEAVTIGEDVSGMPTFCIP VEDGGVGFNYRLHMAIADKWIELLQLKDEDWKMGDIVHTLTNRRWMENCVAYAESHDQALVGDKTIAFWLMDKDMYDFMSLDRPSTPLIDRGIALHKMIR LATMGLGGEGYLNFMGNEFG |
Full Sequence |
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Protein Sequence Length: 863 Download |
MMYYAISGIR LPSVIFKSQS TGSHGTTTTD RITTSGLSFF LKKQPFSRKI FAEKSLSYNS 60 DSSNITVAAA SEKILVPGGE TYDDSSSSPS PKDQLVTNDA VSEEEPQVPN DVDTPTMEDG 120 EDVKDEVEQE KPASLHKTVN IGKSESKPRS IPPPGRGQRI YEIDPSLTSF HQHLDYRYSQ 180 YKRLREEIDK FEGGLDAFSR GYEKFGFTRS ETGITYREWA PGATWAALIG DFNNWNPNAD 240 VMTRNEFGVW EIFLPNNADG SPPIPHGSRV KIRMDTPSGI KDSIPAWIKF SVQAPGEIPY 300 NGIYYDPPEE EKYVFKHSQP KRPKSLRIYE SHVGMSSTEP IINTYANFRD DVLPRIKRLG 360 YNTVQIMAIQ EHSYYASFGY HVTNFFAPSS RFGTPDDLKS LIDKAHELDL LVLMDIVHSH 420 SSNNTLDGLN MFDGTDGHYF HSGSRGYHWM WDSRLFNYGS WEVLRFLLSN ARWWLDEYKF 480 DGFRFDGVTS MMYTHHGLEV AFTGNYNEYF GFATDVDAVV YLMLVNDMIH GLFPEAVTIG 540 EDVSGMPTFC IPVEDGGVGF NYRLHMAIAD KWIELLQLKD EDWKMGDIVH TLTNRRWMEN 600 CVAYAESHDQ ALVGDKTIAF WLMDKDMYDF MSLDRPSTPL IDRGIALHKM IRLATMGLGG 660 EGYLNFMGNE FGHPEWIDFP RGDQHLPSGK IIPGNNFSYD KCRRRFDLGD ADYLRYHGMQ 720 EFDQAMQHLE EAYGFMTSEH QYISRKDEGD RIIVFERGNL VFVFNFHWNN SYSDYQVGCL 780 KPGKYKIVLD SDNSLFGGFS RINHSAEYFS FEGWYDNRPR SFLVYAPSRT AVVYALVEDE 840 KEHLQDADDN KNNNSEHEEP VNG 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 1.0e-10 | 170 | 254 | 91 | + alpha-amylase | ||
PLN03244 | PLN03244 | 3.0e-135 | 262 | 836 | 580 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 93 | 863 | 775 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 309 | 724 | 417 | + 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 | 262 | 837 | 581 | + 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 | ABN05322.1 | 0 | 1 | 842 | 1 | 829 | starch branching enzyme II [Populus trichocarpa] |
GenBank | ABO31358.1 | 0 | 2 | 842 | 1 | 844 | starch branching enzyme II-1 [Malus x domestica] |
GenBank | ACA35286.1 | 0 | 2 | 842 | 1 | 874 | starch branching enzyme I [Cucumis sativus] |
RefSeq | XP_002326414.1 | 0 | 117 | 842 | 1 | 726 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002534111.1 | 0 | 1 | 863 | 1 | 863 | 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 | 3amk_A | 0 | 160 | 845 | 13 | 701 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 160 | 845 | 13 | 701 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 160 | 845 | 13 | 701 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 160 | 845 | 13 | 701 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 1m7x_D | 1.4013e-45 | 212 | 798 | 25 | 577 | 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 |
HO794536 | 709 | 154 | 862 | 0 |
HO777638 | 653 | 210 | 862 | 0 |
HO458123 | 395 | 443 | 837 | 0 |
HO458123 | 304 | 146 | 442 | 0 |
HO777638 | 47 | 163 | 209 | 0.0000000002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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