y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_001595m |
Family | GH13 |
Protein Properties | Length: 853 Molecular Weight: 96691.4 Isoelectric Point: 5.2681 |
Chromosome | Chromosome/Scaffold: 06708 Start: 355942 End: 363395 |
Description | starch branching enzyme 2.1 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 290 | 615 | 2.5e-29 |
LPRIRANNYNTVQLMAVMEHSYYGSFGYHVTNFFAVSSRSGTPEDLKYLIDKAHSLGLSVLMDVVHSHASNNITDGLNGFDVGQSTQDSYFHTGDRGYHK LWDSRLFNYANWEVIRFLLSNLRWWLEEYKFDGFRFDGVTSMLYHHHGINMAFTGDYNEYFSEATDIDAVVYLMLANSLIHNILPDATVIAEDVSGMPGL GRSVSEGGIGFDYRLAMAIPDKWIDYLKNKSDEEWSMKEISWSLTNRRYTEKCVAYAESHDQAIVGDKTVAFLLMDKEMYYGMSCLTDASPMVDRGVALH KMVHLLTMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 853 Download |
MLGSLGLFPA PDFGSLSPSL AKNSKRAVER NCQIVKQKQI ELTGCRKLPG CSRFLFLPRI 60 SIDKRVKQGL AISAAVADEK KTITSFEEDM EITGLLSIDP GLESFKDHFR YRMQRFTNQK 120 QLIEKYEGGL EEFSKGYLKF GFNREAGGIV YREWAPAAQE AQVIGDFNGW DGSNHRMEKN 180 EFGVWSINIP DSGGNPAIHH NSRVKFRFKH GDGVWVDRIP AWIRYATVDP TKFGAPYDGV 240 YWDPPPPERY QFKYPRPPKA QAPRIYEAHV GMSSSEPRIN TYREFADDVL PRIRANNYNT 300 VQLMAVMEHS YYGSFGYHVT NFFAVSSRSG TPEDLKYLID KAHSLGLSVL MDVVHSHASN 360 NITDGLNGFD VGQSTQDSYF HTGDRGYHKL WDSRLFNYAN WEVIRFLLSN LRWWLEEYKF 420 DGFRFDGVTS MLYHHHGINM AFTGDYNEYF SEATDIDAVV YLMLANSLIH NILPDATVIA 480 EDVSGMPGLG RSVSEGGIGF DYRLAMAIPD KWIDYLKNKS DEEWSMKEIS WSLTNRRYTE 540 KCVAYAESHD QAIVGDKTVA FLLMDKEMYY GMSCLTDASP MVDRGVALHK MVHLLTMALG 600 GEGYLNFMGN EFGHPEWIDF PREGNGWSYD KCRRQWNLVD TEHLRYRFMN AFDKAMNLLD 660 EKYSFLASTK QIVSSTNEED KVIVFERGDL VFVFNFHPEN TYDGYKVGCD LPGKYRVALD 720 SDAWEFGGRG RVGHDVDHFT SPEGIPGVPE TNFNNRPNSF KILSAARTCV VYYRVEEKEG 780 NHNSSDIGAA NETLTDIAKL GDFEGINETS PADAVAKQED LKAAQPSLIA DDIATKANTE 840 TEEIEEETSD DK* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 4.0e-8 | 105 | 191 | 93 | + alpha-amylase | ||
PLN03244 | PLN03244 | 3.0e-140 | 196 | 735 | 545 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 71 | 796 | 726 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 246 | 654 | 409 | + 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 | 196 | 735 | 542 | + 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 | 19 | 824 | 17 | 807 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 1 | 852 | 1 | 852 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 1 | 851 | 1 | 840 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 34 | 851 | 12 | 817 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002510672.1 | 0 | 1 | 852 | 49 | 895 | 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 | 83 | 777 | 1 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 83 | 777 | 1 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 83 | 777 | 1 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 83 | 777 | 1 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 1.4013e-45 | 148 | 728 | 26 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch biosynthesis | RXN-7710 | EC-2.4.1.18 | 1,4-α-glucan branching enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO619167 | 602 | 179 | 779 | 0 |
HO794536 | 697 | 95 | 779 | 0 |
HO777638 | 645 | 147 | 779 | 0 |
CX109187 | 386 | 392 | 777 | 0 |
HO777638 | 47 | 98 | 144 | 0.33 |
Sequence Alignments (This image is cropped. Click for full image.) |
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