y
Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si008087m |
Family | GH13 |
Protein Properties | Length: 692 Molecular Weight: 80216.3 Isoelectric Point: 6.105 |
Chromosome | Chromosome/Scaffold: 4 Start: 20265008 End: 20274133 |
Description | Alpha amylase family protein |
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 | 429 | 691 | 4.6e-24 |
FQEFTSKVLPHIKNAGYNAVQLIGVVEHKDYSSVGYKVTNYFAVSSRFGTPDDFKKLVDEAHGLGLVVLLDIVHSYASADELVGLSLFDGSNDCYFHSGK RGHHKYWGTRMFKYDDVDVLHFLLSNLNWWVTEYRIDGFQFHSLSSMLYTHNGFSTFTGTMEEYCNQYVDKDAIIYLILANEMLHDLHPDIITIAEDATF YPGLCEPTTQGGLGFDYCVNLSVPEMWLWHLENVPEREWSMNKIMKVLVSSDQKMLSYVENHN |
Full Sequence |
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Protein Sequence Length: 692 Download |
MSSCPLFLMT PRPPPLLVHA DRYPPIGSAY LPTSRRPCPG RRHGYLFRCD SSSSSSAPRD 60 RTPRPRQQRQ RSQRPGGRRV DAVDPVGFLA KLRVSDRAFA QFLRDRHKAL KDRRWELCSR 120 FIDLKEVSSG FELLGMHRHR QHRMDFMEWA PGARYCSLVG DFNEWSPTEN CAREGHLGHD 180 DFGYWFIILE DKLREGQEPD EYFFQEYNYV DDYDKGDNGV DAEEIMHRMK EEYWEPGEIR 240 SHKSQLEMVV KLYEQMFGPN GPQTEEELGE IPDAQTRYNE WKALQKTDLS SMSPSYDIID 300 SGQPFDIFNV VTDGASFEKF QAKKPPLAYW VEMRKGRIAW LEKYVPTISH KDKYRVYFNT 360 PDGALERVPA WATYVLPDAE GKQSYAVHWE PPPEEVYQWR FGRPKVKGSL RIYESHVGIS 420 GSEEKVSSFQ EFTSKVLPHI KNAGYNAVQL IGVVEHKDYS SVGYKVTNYF AVSSRFGTPD 480 DFKKLVDEAH GLGLVVLLDI VHSYASADEL VGLSLFDGSN DCYFHSGKRG HHKYWGTRMF 540 KYDDVDVLHF LLSNLNWWVT EYRIDGFQFH SLSSMLYTHN GFSTFTGTME EYCNQYVDKD 600 AIIYLILANE MLHDLHPDII TIAEDATFYP GLCEPTTQGG LGFDYCVNLS VPEMWLWHLE 660 NVPEREWSMN KIMKVLVSSD QKMLSYVENH NQ 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 2.0e-9 | 97 | 191 | 95 | + 1,4-alpha-glucan-branching enzyme | ||
PLN02447 | PLN02447 | 4.0e-134 | 345 | 692 | 354 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 1.0e-135 | 393 | 692 | 303 | + 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 | 1 | 692 | 696 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 82 | 692 | 616 | + alpha-amylase; Provisional |
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 |
EMBL | CBI26672.1 | 0 | 25 | 692 | 20 | 680 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001057611.1 | 0 | 1 | 692 | 1 | 686 | Os06g0367100 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001108121.1 | 0 | 1 | 692 | 1 | 683 | starch branching enzyme III [Zea mays] |
RefSeq | NP_001154629.1 | 0 | 64 | 692 | 47 | 683 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002455921.1 | 0 | 1 | 692 | 1 | 690 | hypothetical protein SORBIDRAFT_03g027310 [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 | 346 | 692 | 114 | 469 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 346 | 692 | 114 | 469 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 346 | 692 | 114 | 469 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
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 |
FE606762 | 240 | 137 | 376 | 0 |
BF272517 | 278 | 367 | 644 | 0 |
JG636329 | 270 | 354 | 623 | 0 |
CB644230 | 255 | 131 | 385 | 0 |
CO104525 | 273 | 394 | 666 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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