Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00067040m |
Family | GH13 |
Protein Properties | Length: 826 Molecular Weight: 93653.2 Isoelectric Point: 6.6176 |
Chromosome | Chromosome/Scaffold: 020564 Start: 1566 End: 7766 |
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 | 279 | 604 | 3e-27 |
LPRIRANNYNTVQLMAVMEHSYYASFGYHVTNFFAVSSRSGTPEDLKYLVDKAHSLGLRVLMDVVHSHASNNVTDGLNGYDVGQSTQESYFHTGDRGYHK LWDSRLFNYANWEVLRFLLSNLRYWMDEFMFDGFRFDGVTSMLYHHHGINVGFTGNYKEYFSLDTDVDAVVYMMLANHLMHKILPEATVVAEDVSGMPVL CRPVDEGGVGFDYRLAMAIPDRWIDYLKNKEDSEWSMGEIAHTLTNRRYTEKCIAYAESHDQSIVGDKTIAFLLMDKEMYTGMSDLQPASPTIDRGIALQ KMIHFITMALGGDGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 826 Download |
MLCITSPSSS PAPLQPARRS RALSDRAAPP RIAGGGNVRL SVLSVQREAR RPGPAKAKSK 60 FATAATVQED KTMAASKDNV DHLPIYKLDP KLEEFKDHFS YRMKRYLDQK CSIEKNEGSL 120 EEFSKGYLKY GINTNKDGTV YREWAPAAQE AQLIGDFNDW NGANHQMEKD QFGVWSIKID 180 HVKGKPAIPH NSRVKFRFRH GAVWADRIPA WIHYAAVDAS KFGAPYDGVH WDPPASERYM 240 FKHPRPSKPD APRIYEAHVG MSGEKPAVST YREFADNVLP RIRANNYNTV QLMAVMEHSY 300 YASFGYHVTN FFAVSSRSGT PEDLKYLVDK AHSLGLRVLM DVVHSHASNN VTDGLNGYDV 360 GQSTQESYFH TGDRGYHKLW DSRLFNYANW EVLRFLLSNL RYWMDEFMFD GFRFDGVTSM 420 LYHHHGINVG FTGNYKEYFS LDTDVDAVVY MMLANHLMHK ILPEATVVAE DVSGMPVLCR 480 PVDEGGVGFD YRLAMAIPDR WIDYLKNKED SEWSMGEIAH TLTNRRYTEK CIAYAESHDQ 540 SIVGDKTIAF LLMDKEMYTG MSDLQPASPT IDRGIALQKM IHFITMALGG DGYLNFMGNE 600 FGHPEWIDFP REGNNWSYDK CRRQWSLVDT DHLRYKYMDA FDQAMNALDE EFFFLSSPKQ 660 IVSDMNEEKK VIVFERGDLV FVFNFHPKKT YDGYKVGCDL PGKYRVALDS DAFVFGGHGR 720 VGHDVDHFTS PEGVPGVPET NFNNRPNSFK VLSPPRTCVA YYRVDEEAET TGAGKTSPEI 780 IDVDATPLKT PTATTEAHEE RESTEDVSSK KGRQFGRQSS DKSTK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 5.0e-6 | 102 | 180 | 85 | + alpha-amylase | ||
PLN03244 | PLN03244 | 8.0e-134 | 186 | 711 | 528 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 4.0e-180 | 186 | 711 | 527 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 68 | 769 | 703 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 236 | 643 | 408 | + 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. |
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 | AAD50279.2 | 0 | 1 | 825 | 1 | 832 | seed starch branching enzyme [Sorghum bicolor] |
GenBank | AAO20100.1 | 0 | 1 | 825 | 1 | 823 | starch branching enzyme I [Zea mays] |
GenBank | ABQ15209.1 | 0 | 1 | 825 | 1 | 823 | starch branching enzyme I [Zea mays] |
DDBJ | BAA01854.1 | 0 | 2 | 825 | 1 | 822 | branching enzyme-I precursor [Zea mays] |
RefSeq | NP_001105370.1 | 0 | 1 | 825 | 1 | 823 | starch branching enzyme1 [Zea mays] |
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 | 73 | 825 | 1 | 755 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 73 | 769 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 73 | 769 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 73 | 769 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 3.00018e-42 | 138 | 717 | 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 | 610 | 169 | 773 | 0 |
HO794536 | 717 | 85 | 782 | 0 |
HO777638 | 664 | 138 | 782 | 0 |
CX109187 | 452 | 381 | 826 | 0 |
HO458123 | 401 | 372 | 761 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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