y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_001701m |
Family | GH13 |
Protein Properties | Length: 834 Molecular Weight: 95605.4 Isoelectric Point: 5.7044 |
Chromosome | Chromosome/Scaffold: 12513 Start: 202686 End: 222012 |
Description | starch branching enzyme 2.2 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 340 | 660 | 7.5e-28 |
LPRIKKLGYNAVQLMAIQEHSYYASFGYHVTNFYAASSRFGTPDDLKSLIDKAHELDLLVLMDIVHSHASTNTLDGLNMFDGTDGHYFHSGPRGHHWMWD SRLFNYGSWEVLRFLLSNARWWLDEYKFDGFRFDGVTSMMYTHHGLQVDFTGNYNEYFGYATDVDAVVYLMLLNDMIHGLFPEAVTIGEDVSGMPTVCIP VEDGGVGFDYRLHMAVADKWVEIIQKRDEDWKMGDIVHMLTNRRWLEKCVSYAESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPLIDRGVALHKMIR LITMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 834 Download |
MGHYTISGIR FPCAPLCKSQ STGFHGDRRT SSCLSFNFKK EAFSRRVFSG KSSHESDSSN 60 VMVTASKRVL PDGRIECYSS STDQLEAPGT VSEESQVLTD VESLIMDDKI VEDEVNKESV 120 PMRETVSIRK IGSKPRSIPP PGRGQRIYDI DPSLTGFRQH LDYRYSQYKR LREEIDKYEG 180 SLDAFSRGYE KFGFSRSETG ITYREWAPGA TWAALIGDFN NWNPNADVMT QNECGVWEIF 240 LPNNADGSPP IPHGSRVKIR MDTPSGNKDS IPAWIKFSVQ APGELPYNGI YYDPPEEEKY 300 VFKNPQPKRP KSLRIYESHV GMSSTEPVIN TYANFRDDVL PRIKKLGYNA VQLMAIQEHS 360 YYASFGYHVT NFYAASSRFG TPDDLKSLID KAHELDLLVL MDIVHSHAST NTLDGLNMFD 420 GTDGHYFHSG PRGHHWMWDS RLFNYGSWEV LRFLLSNARW WLDEYKFDGF RFDGVTSMMY 480 THHGLQVDFT GNYNEYFGYA TDVDAVVYLM LLNDMIHGLF PEAVTIGEDV SGMPTVCIPV 540 EDGGVGFDYR LHMAVADKWV EIIQKRDEDW KMGDIVHMLT NRRWLEKCVS YAESHDQALV 600 GDKTIAFWLM DKDMYDFMAL DRPSTPLIDR GVALHKMIRL ITMGLGGEGY LNFMGNEFGH 660 PEWIDFPRGD LHLPSGKFVP GNNYSYDKCR RRFDLHLRYH GMQEFDQAIQ HLEEAYGFMT 720 SEHQYISRKD ERDRIIVFER GNLVFVFNFH WTSSYSDYRV GCLKPGKYKI VLDSDDPLFG 780 GFGRLSHDAE HFSFEGWYDN RPRSFMVYTP CRTAVVYALV EDEVENEVEP VAG* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 7.0e-10 | 157 | 224 | 69 | + alpha-amylase | ||
PLN03244 | PLN03244 | 2.0e-138 | 249 | 819 | 582 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 64 | 819 | 764 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 296 | 707 | 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 | 249 | 819 | 577 | + 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 | 825 | 1 | 829 | starch branching enzyme II [Populus trichocarpa] |
GenBank | ABO31358.1 | 0 | 5 | 821 | 4 | 840 | starch branching enzyme II-1 [Malus x domestica] |
GenBank | ACA35286.1 | 0 | 4 | 825 | 3 | 874 | starch branching enzyme I [Cucumis sativus] |
RefSeq | XP_002326414.1 | 0 | 107 | 825 | 3 | 726 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002534111.1 | 0 | 1 | 826 | 1 | 843 | 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 | 147 | 825 | 13 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 147 | 825 | 13 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 147 | 825 | 13 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 147 | 825 | 13 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 1m7x_D | 0 | 199 | 781 | 25 | 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 |
HO794536 | 683 | 141 | 819 | 0 |
HO777638 | 627 | 197 | 819 | 0 |
HO458123 | 393 | 430 | 818 | 0 |
HO458123 | 296 | 141 | 429 | 0 |
HO777638 | 47 | 150 | 196 | 0.0000000001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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