Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_027_00415.5 |
Family | GH13 |
Protein Properties | Length: 656 Molecular Weight: 75437 Isoelectric Point: 5.2849 |
Chromosome | Chromosome/Scaffold: 27 Start: 3334460 End: 3351617 |
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 | 170 | 490 | 5.2e-28 |
LPRIKMLGYNAVQLMAIQEHSYYASFGYHVTNFFAPSSRCGTPDDLKSLIDKAHELGLLVLMDIVHSHASNNVLDGLNMFDGTDGQYFHSGARGYHWMWD SRLFNYGSWEVLRFLLSNARWWLDEYKFDGFRFDGVTSMMYTHHGLQMAFTGNYDEYFGLATDVDAVVYLMLVNDLIHGLFPEAVTVGEDVSGMPTFGIP VQDGGVGFDYRLHMAVADKWIELLKKRDEDWQMGDIVHTLTNRRWSEKCVVYAESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPLIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 656 Download |
MREEIDKYEG GLEIFSRGYE KLGFNRSTTG VTYREWAPGA KSASLIGDFN NWNPNADVMT 60 QNEFGVWEVF LPNNADGSSP IPHGSRVKIH MDTPTGIKDS IPAWIRFSVQ APGEIPYNGI 120 YYDPPEEERY VFQHPRPKRP KSLRIYEAHV GMSSTEPKIN TYAEFRDDVL PRIKMLGYNA 180 VQLMAIQEHS YYASFGYHVT NFFAPSSRCG TPDDLKSLID KAHELGLLVL MDIVHSHASN 240 NVLDGLNMFD GTDGQYFHSG ARGYHWMWDS RLFNYGSWEV LRFLLSNARW WLDEYKFDGF 300 RFDGVTSMMY THHGLQMAFT GNYDEYFGLA TDVDAVVYLM LVNDLIHGLF PEAVTVGEDV 360 SGMPTFGIPV QDGGVGFDYR LHMAVADKWI ELLKKRDEDW QMGDIVHTLT NRRWSEKCVV 420 YAESHDQALV GDKTIAFWLM DKDMYDFMAL DRPSTPLIDR GIALHKMIRL ITMGLGGEGY 480 LNFMGNEFGH PEWIDFPRGE QHLPDGRVIP GNNNSYDKCR RRFDLGDAEY LRYHGMQQFD 540 QAMQHLEDRY GFMTSQHQYI SRKDEGDRVI VFERGDLVFV FNFHWTTSYS DYRVGCLKPG 600 KYKVVLDSDS KLFGGFNRID PDADYFSMEG MYDNRPNSFM LYTPCRTAVV YALVD* 660 |
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 | 1 | 71 | 77 | + alpha-amylase | ||
PLN03244 | PLN03244 | 3.0e-140 | 81 | 653 | 581 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 1 | 655 | 659 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 126 | 541 | 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 | 81 | 654 | 579 | + 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 | 655 | 171 | 825 | starch branching enzyme II [Populus trichocarpa] |
GenBank | ABO31359.1 | 0 | 1 | 655 | 186 | 840 | starch branching enzyme II-2 [Malus x domestica] |
EMBL | CAA56319.1 | 0 | 1 | 655 | 192 | 846 | starch branching enzyme I [Pisum sativum] |
RefSeq | XP_002277213.1 | 0 | 1 | 652 | 407 | 1058 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002326414.1 | 0 | 1 | 655 | 68 | 722 | predicted protein [Populus trichocarpa] |
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 | 5 | 655 | 41 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 5 | 655 | 41 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 5 | 655 | 41 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 5 | 655 | 41 | 694 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 1m7x_D | 0 | 17 | 617 | 9 | 579 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 655 | 1 | 655 | 0 |
HO777638 | 629 | 27 | 655 | 0 |
HO458123 | 395 | 260 | 654 | 0 |
HO458123 | 265 | 2 | 259 | 0 |
HO777638 | 26 | 1 | 26 | 9.9 |
Sequence Alignments (This image is cropped. Click for full image.) |
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