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Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_002172m |
Family | GH13 |
Protein Properties | Length: 764 Molecular Weight: 86958 Isoelectric Point: 4.9501 |
Chromosome | Chromosome/Scaffold: 06708 Start: 356301 End: 363178 |
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 | 201 | 526 | 1.6e-29 |
LPRIRANNYNTVQLMAVMEHSYYGSFGYHVTNFFAVSSRSGTPEDLKYLIDKAHSLGLSVLMDVVHSHASNNITDGLNGFDVGQSTQDSYFHTGDRGYHK LWDSRLFNYANWEVIRFLLSNLRWWLEEYKFDGFRFDGVTSMLYHHHGINMAFTGDYNEYFSEATDIDAVVYLMLANSLIHNILPDATVIAEDVSGMPGL GRSVSEGGIGFDYRLAMAIPDKWIDYLKNKSDEEWSMKEISWSLTNRRYTEKCVAYAESHDQAIVGDKTVAFLLMDKEMYYGMSCLTDASPMVDRGVALH KMVHLLTMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 764 Download |
MEITGLLSID PGLESFKDHF RYRMQRFTNQ KQLIEKYEGG LEEFSKGYLK FGFNREAGGI 60 VYREWAPAAQ EAQVIGDFNG WDGSNHRMEK NEFGVWSINI PDSGGNPAIH HNSRVKFRFK 120 HGDGVWVDRI PAWIRYATVD PTKFGAPYDG VYWDPPPPER YQFKYPRPPK AQAPRIYEAH 180 VGMSSSEPRI NTYREFADDV LPRIRANNYN TVQLMAVMEH SYYGSFGYHV TNFFAVSSRS 240 GTPEDLKYLI DKAHSLGLSV LMDVVHSHAS NNITDGLNGF DVGQSTQDSY FHTGDRGYHK 300 LWDSRLFNYA NWEVIRFLLS NLRWWLEEYK FDGFRFDGVT SMLYHHHGIN MAFTGDYNEY 360 FSEATDIDAV VYLMLANSLI HNILPDATVI AEDVSGMPGL GRSVSEGGIG FDYRLAMAIP 420 DKWIDYLKNK SDEEWSMKEI SWSLTNRRYT EKCVAYAESH DQAIVGDKTV AFLLMDKEMY 480 YGMSCLTDAS PMVDRGVALH KMVHLLTMAL GGEGYLNFMG NEFGHPEWID FPREGNGWSY 540 DKCRRQWNLV DTEHLRYRFM NAFDKAMNLL DEKYSFLAST KQIVSSTNEE DKVIVFERGD 600 LVFVFNFHPE NTYDGYKVGC DLPGKYRVAL DSDAWEFGGR GRVGHDVDHF TSPEGIPGVP 660 ETNFNNRPNS FKILSAARTC VVYYRVEEKE GNHNSSDIGA ANETLTDIAK LGDFEGINET 720 SPADAVAKQE DLKAAQPSLI ADDIATKANT ETEEIEEETS DDK* 780 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 5.0e-8 | 16 | 102 | 93 | + alpha-amylase | ||
PLN03244 | PLN03244 | 5.0e-140 | 107 | 646 | 545 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 1 | 707 | 707 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 157 | 565 | 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 | 107 | 646 | 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 | 1 | 735 | 89 | 807 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 1 | 763 | 90 | 852 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 2 | 762 | 94 | 840 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 2 | 762 | 71 | 817 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002510672.1 | 0 | 1 | 763 | 135 | 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 | 6 | 688 | 13 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 6 | 688 | 13 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 6 | 688 | 13 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 6 | 688 | 13 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 0 | 59 | 639 | 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 | 90 | 690 | 0 |
HO794536 | 697 | 6 | 690 | 0 |
HO777638 | 690 | 13 | 690 | 0 |
CX109187 | 386 | 303 | 688 | 0 |
HO777638 | 47 | 9 | 55 | 0.06 |
Sequence Alignments (This image is cropped. Click for full image.) |
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