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Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb04g021540.1 |
Family | GH13 |
Protein Properties | Length: 804 Molecular Weight: 90755.1 Isoelectric Point: 6.3045 |
Chromosome | Chromosome/Scaffold: 4 Start: 50589774 End: 50601467 |
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 | 318 | 638 | 8e-33 |
LPRIKKLGYNAVQIMAIQEHSYYGSFGYHVTNFFAPSSRFGTPEDLKSMIDRAHELGLLVLMDVVHSHASSNTLDGLNGFDGTDTHYFHSGPRGHHWMWD SRLFNYGNWEVLRFLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVTFTGNFNEYFGFATDVDAVVYLMLVNDLIHGLYPEAVTIGEDVSGMPTFALP VQDGGVGFDYRMHMAVADKWIELLKQSDEAWKMGDIVHTLTNRRWLEKCVTYAESHDQALVGDKTIAFWLMDKDMYDFMALDRPATPTIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 804 Download |
MAAFAVSGAA LGGAVRAPRL TGGEEGSLVF RRTGPFLTRA GGARVGGSGT HGAMRAAAAS 60 SRKAVVVAEG ENDGLASKAD SAQFQSDELE VPDVTEETMC DAGVADAQAL NRVRVVPPPS 120 DGQKIFQIDP MLQGYKYHLE YRYSLYRRIR SDIDEHEGGL EAFSRSYEKF GFNRSAEGIT 180 YREWAPGALS AALVGDFNNW DPNADRMSKN EFGVWEIFLP NNADGTSPIP HGTRVKVRMD 240 TPSGIKDSIP AWIKYSVQAP GEIPYDGLYY DPPEEVKYVF KHPKPKRPKS LRIYETHVGM 300 SSPEPKINTY ANFRDEVLPR IKKLGYNAVQ IMAIQEHSYY GSFGYHVTNF FAPSSRFGTP 360 EDLKSMIDRA HELGLLVLMD VVHSHASSNT LDGLNGFDGT DTHYFHSGPR GHHWMWDSRL 420 FNYGNWEVLR FLLSNARWWL EEYKFDGFRF DGVTSMMYTH HGLQVTFTGN FNEYFGFATD 480 VDAVVYLMLV NDLIHGLYPE AVTIGEDVSG MPTFALPVQD GGVGFDYRMH MAVADKWIEL 540 LKQSDEAWKM GDIVHTLTNR RWLEKCVTYA ESHDQALVGD KTIAFWLMDK DMYDFMALDR 600 PATPTIDRGI ALHKMIRLIT MGLGGEGYLN FMGNEFGHPE WIDFPRGPQR LPSGKFIPGN 660 NNSYDKCRRR FDLGDADYLR YRGMQEFDQA MQHLEQKYGF MTSDHQYISR KHEEDKMIVF 720 EKGDLVFVFN FHCNNSYFDY RIGCRKPGMY KVVLDSDAGL FGGFGRIHHA AEHFTTDCSH 780 DNRPHSFSVY TPSRTCVVYA PAE* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 2.0e-8 | 139 | 219 | 87 | + alpha-amylase | ||
PLN03244 | PLN03244 | 6.0e-134 | 229 | 799 | 580 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 69 | 803 | 739 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 273 | 689 | 418 | + 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 | 229 | 799 | 575 | + 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 | AAC33764.1 | 0 | 3 | 803 | 2 | 799 | starch branching enzyme IIb [Zea mays] |
GenBank | AAP72267.1 | 0 | 1 | 803 | 1 | 803 | starch branching enzyme IIb [Sorghum bicolor] |
GenBank | ABO25741.1 | 0 | 3 | 803 | 2 | 799 | starch branching enzyme IIb [Zea mays] |
RefSeq | NP_001105316.1 | 0 | 3 | 803 | 2 | 799 | amylose extender1 precursor [Zea mays] |
RefSeq | XP_002453926.1 | 0 | 1 | 803 | 1 | 803 | hypothetical protein SORBIDRAFT_04g021540 [Sorghum bicolor] |
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 | 121 | 799 | 9 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 121 | 799 | 9 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 121 | 799 | 9 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 121 | 799 | 9 | 690 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 1m7x_D | 0 | 165 | 797 | 9 | 610 | 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 | 685 | 119 | 803 | 0 |
HO777638 | 629 | 175 | 803 | 0 |
HO458123 | 392 | 411 | 802 | 0 |
HO458123 | 290 | 119 | 407 | 0 |
HO777638 | 47 | 128 | 174 | 0.000005 |
Sequence Alignments (This image is cropped. Click for full image.) |
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