Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si006006m |
Family | GH13 |
Protein Properties | Length: 671 Molecular Weight: 75577.7 Isoelectric Point: 8.5654 |
Chromosome | Chromosome/Scaffold: 4 Start: 39908082 End: 39911892 |
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 | 346 | 657 | 1.7e-27 |
LPRIRANNYNTVQLMAVMEHSYYASFGYHVTNFFAVSSRSGTPEDLKYLVDKAHSLGLRVLMDVVHSHASNNVTDGLNGYDVGQNTHESYFHTGDRGYHK LWDSRLFNYANWEVLRFLLSNLRYWMHEFMFDGFRFDGVTSMLYHHHGINVGFTGNYKEYFSLDTDVDAVVYMMLANHLMHKILPEATVVAEDVSGMPVL CRPVDEGGVGFDYRLAMAIPDRWIDYLKNKDDSEWSMGEIAHTLTNRRYTEKCIAYAESHDQSIVGDKTIAFLLMDKEMYTGMSDLQPASPTIDRGIALQ KMIHFITMALGG |
Full Sequence |
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Protein Sequence Length: 671 Download |
MASPSLLSGG GGSRGRLRRR RKPKKITPSL RGREEVEGGK DANPAPAPAI KLEELPVLTR 60 WDSLAAEMLC ITSSSSSPVP LQPTRRPRAP SDRAAPPGIA GGGNVRLSVL SVQRDVRRSG 120 PAKAKSKFAT AATVQENKTM EATKDDVNHL PIYKLDPKLE KFKDHFSYRM KRYLEQKSSI 180 EKNEGGLEEF SKGYLKFGIN TNKDGTVYRE WAPAAQEAQL VGDFNDWNGA NHNMKKDKFG 240 VWSIKIDHVK GEPAIPHNSR VKFRFKHGGV WVDRIPAWIR YATVDASKFG APYDGVHWDP 300 PASERYVFMY PRPPKPDAPR IYEAHVGMSG EEPAVSTYRE FADNVLPRIR ANNYNTVQLM 360 AVMEHSYYAS FGYHVTNFFA VSSRSGTPED LKYLVDKAHS LGLRVLMDVV HSHASNNVTD 420 GLNGYDVGQN THESYFHTGD RGYHKLWDSR LFNYANWEVL RFLLSNLRYW MHEFMFDGFR 480 FDGVTSMLYH HHGINVGFTG NYKEYFSLDT DVDAVVYMML ANHLMHKILP EATVVAEDVS 540 GMPVLCRPVD EGGVGFDYRL AMAIPDRWID YLKNKDDSEW SMGEIAHTLT NRRYTEKCIA 600 YAESHDQSIV GDKTIAFLLM DKEMYTGMSD LQPASPTIDR GIALQKMIHF ITMALGGDGY 660 LNFMGNEVKS * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 6.0e-6 | 135 | 247 | 119 | + alpha-amylase | ||
PLN03244 | PLN03244 | 1.0e-105 | 253 | 667 | 417 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 4.0e-139 | 253 | 667 | 416 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 135 | 667 | 534 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 303 | 667 | 365 | + 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 | 68 | 667 | 1 | 600 | seed starch branching enzyme [Sorghum bicolor] |
GenBank | AAO20100.1 | 0 | 68 | 667 | 1 | 600 | starch branching enzyme I [Zea mays] |
DDBJ | BAA01854.1 | 0 | 69 | 667 | 1 | 599 | branching enzyme-I precursor [Zea mays] |
RefSeq | NP_001105370.1 | 0 | 68 | 667 | 1 | 600 | starch branching enzyme1 [Zea mays] |
RefSeq | XP_002439059.1 | 0 | 68 | 667 | 1 | 600 | hypothetical protein SORBIDRAFT_10g030776 [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 | 3aml_A | 0 | 140 | 667 | 1 | 529 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 140 | 667 | 1 | 529 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 140 | 667 | 1 | 529 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 140 | 667 | 1 | 529 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 3e-35 | 205 | 615 | 26 | 424 | 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 | 434 | 236 | 667 | 0 |
HO794536 | 517 | 152 | 667 | 0 |
HO777638 | 464 | 205 | 667 | 0 |
EC365731 | 289 | 307 | 595 | 0 |
HO777638 | 45 | 155 | 199 | 0.79 |
Sequence Alignments (This image is cropped. Click for full image.) |
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