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Basic Information | |
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Species | Mimulus guttatus |
Cazyme ID | mgv1a001301m |
Family | GH13 |
Protein Properties | Length: 845 Molecular Weight: 95692.7 Isoelectric Point: 5.1403 |
Chromosome | Chromosome/Scaffold: 210 Start: 262856 End: 271703 |
Description | starch branching enzyme 2.2 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 345 | 666 | 1.1e-29 |
LPRIKKLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPDDLKSLIDKAHELGLVVLMDIVHSHSSNNTLDGLNMFDGTDSCYFHSGTRGYHWMWD SRLFNYGQWEVLRFLLSNARWWLDEYKFDGFRFDGVTSMMYTHHGLQMAFTGNYSEYFGFATDVDAVAYLMLVNDLIHGLFPEAITIGEDVSGMPAFCIP LQDGGMGFDYRLHMAIADKWIETLKKRDEEWSMGDIIHTLTNRRWREKCVCYAESHDQALVGDKTIAFWLMDKDMYDFMAVDRPSTPLIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 845 Download |
MVYTLPGVRL PTVPSAAYKV GSCGMIFSGG KAYESGFQPS MATAPEKVLV PGTESDGSSS 60 PRENLEIVSG TSQACNLESV DGPIVKEQEQ LIEQQISGEA IKGKDSASVQ LLDEDAGLNT 120 EGKSYSISKT IADESSMVKE RVIPPPGAGQ KIYEIDTLLT NYREHLDYRY GQYKKLRDAI 180 DKYEGGLEVF SRGYEKLGFN RSETGITYRE WAPGAKSASL IGDFNNWNAN ADVMTRNEFG 240 VWEIFLPNNA DGSPAIPHGS RVKIRMDTPS GIKDSIPAWI KFSVQAPGEI PYNGIYYDPP 300 VEERYVFKHP RPSKPKSLRI YECHVGMSST EPVINTYANF RDEVLPRIKK LGYNAVQIMA 360 IQEHSYYASF GYHVTNFFAP SSRFGTPDDL KSLIDKAHEL GLVVLMDIVH SHSSNNTLDG 420 LNMFDGTDSC YFHSGTRGYH WMWDSRLFNY GQWEVLRFLL SNARWWLDEY KFDGFRFDGV 480 TSMMYTHHGL QMAFTGNYSE YFGFATDVDA VAYLMLVNDL IHGLFPEAIT IGEDVSGMPA 540 FCIPLQDGGM GFDYRLHMAI ADKWIETLKK RDEEWSMGDI IHTLTNRRWR EKCVCYAESH 600 DQALVGDKTI AFWLMDKDMY DFMAVDRPST PLIDRGIALH KMIRLITMGL GGEGYLNFMG 660 NEFGHPEWID FPRGDQHLPD GRVIPGNGNS YDKCRRRFDL GDAEYLRYHG LQEFDQAMQH 720 LEENYGFMTS EHQYISRKDE ADRVIVFERG NLLFVFNFHW SKSYSDYRVG CLKPGKYKVA 780 LDSDDKLFGG FGRISHEAEY FTSEGWQDDR PRSFYIYAPS RTAVVYALAE VEAEPIDVQV 840 SPNV* 900 |
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 | 169 | 246 | 84 | + alpha-amylase | ||
PLN03244 | PLN03244 | 1.0e-141 | 254 | 822 | 577 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 93 | 822 | 734 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 302 | 716 | 416 | + 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 | 254 | 822 | 574 | + 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 |
DDBJ | BAB64912.1 | 0 | 1 | 837 | 1 | 867 | starch branching enzyme II [Ipomoea batatas] |
EMBL | CAA56319.1 | 0 | 1 | 838 | 1 | 855 | starch branching enzyme I [Pisum sativum] |
EMBL | CAB40743.1 | 0 | 1 | 837 | 1 | 870 | starch branching enzyme II [Solanum tuberosum] |
EMBL | CAB40746.1 | 0 | 1 | 830 | 1 | 858 | starch branching enzyme II [Solanum tuberosum] |
EMBL | CAB40747.1 | 0 | 26 | 827 | 1 | 810 | starch branching enzyme II [Solanum tuberosum] |
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 | 152 | 836 | 13 | 700 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 152 | 836 | 13 | 700 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 152 | 836 | 13 | 700 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 152 | 836 | 13 | 700 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3k1d_A | 0 | 204 | 824 | 136 | 717 | A Chain A, Crystal Structure Of Glycogen Branching Enzyme Synonym: 1,4- Glucan:1,4-Alpha-D-Glucan 6-Glucosyl-Transferase From Mycob Tuberculosis H3 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 677 | 146 | 822 | 0 |
HO777638 | 621 | 202 | 822 | 0 |
HO458123 | 388 | 435 | 822 | 0 |
HO458123 | 294 | 146 | 434 | 0 |
HO777638 | 47 | 155 | 201 | 0.00000002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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