y
Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb06g015110.1 |
Family | GH13 |
Protein Properties | Length: 416 Molecular Weight: 47652.5 Isoelectric Point: 5.8295 |
Chromosome | Chromosome/Scaffold: 6 Start: 42231120 End: 42234405 |
Description | alpha-amylase-like 2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 46 | 335 | 3.5e-34 |
EEKVTDLAESGFTSVWLPPPTQSLSREGYLPQNLYCLDSCYGSLHELKSLLHKMSEHNVRAMADVVLNHRIGTTQGSNGMYNRYDGIPISWDEHAVTSCS GGKGNKSTGDNFDGVPNIDHTQPFVRKDIIEWLIWLRKSVGFQDFRFDFTKGYAAKFVKEYIEESKPLFAVGEYWDSCEYSPPDYRLNYNQDSHRQKIIN WIDNTGGLCAAFDFTTKGILQEAVKGELWRLRDPEGKPPGVMGWWPSRSVTFIENHDTGSTQGHWPFPSDHIMEGYAYILTHPGIPTVFY |
Full Sequence |
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Protein Sequence Length: 416 Download |
MGQMVSDDKF EEQAARDGGI IKNGREILFQ AFNWESNKHN WWRNLEEKVT DLAESGFTSV 60 WLPPPTQSLS REGYLPQNLY CLDSCYGSLH ELKSLLHKMS EHNVRAMADV VLNHRIGTTQ 120 GSNGMYNRYD GIPISWDEHA VTSCSGGKGN KSTGDNFDGV PNIDHTQPFV RKDIIEWLIW 180 LRKSVGFQDF RFDFTKGYAA KFVKEYIEES KPLFAVGEYW DSCEYSPPDY RLNYNQDSHR 240 QKIINWIDNT GGLCAAFDFT TKGILQEAVK GELWRLRDPE GKPPGVMGWW PSRSVTFIEN 300 HDTGSTQGHW PFPSDHIMEG YAYILTHPGI PTVFYDHFYD QGVPLHDEIA KLMQIRKCQD 360 IHSRSSIKIL EVRSDLYSAI IDDKLCMKIG DGSWCPSDPE WMLAVSGDRY AVWHK* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 2.0e-46 | 23 | 357 | 418 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 5.0e-143 | 26 | 415 | 406 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-159 | 27 | 367 | 345 | + Alpha amylase catalytic domain found in archaeal, bacterial, and plant Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes AmyA from bacteria, archaea, water fleas, and plants. 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. | ||
PLN02784 | PLN02784 | 2.0e-169 | 23 | 415 | 400 | + alpha-amylase | ||
PLN02361 | PLN02361 | 0 | 15 | 415 | 401 | + alpha-amylase |
Gene Ontology | |
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GO Term | Description |
GO:0004556 | alpha-amylase activity |
GO:0005509 | calcium ion binding |
GO:0005975 | carbohydrate metabolic process |
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 | CAE02023.2 | 0 | 4 | 415 | 1 | 412 | OSJNBb0118P14.5 [Oryza sativa (japonica cultivar-group)] |
EMBL | CAX51375.1 | 0 | 1 | 415 | 1 | 415 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
RefSeq | NP_001052697.1 | 0 | 2 | 415 | 31 | 444 | Os04g0403300 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001141482.1 | 0 | 1 | 415 | 1 | 415 | hypothetical protein LOC100273593 [Zea mays] |
RefSeq | XP_002446386.1 | 0 | 1 | 415 | 1 | 415 | hypothetical protein SORBIDRAFT_06g015110 [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 | 1bg9_A | 0 | 26 | 415 | 1 | 402 | A Chain A, Crystal Structure Of The C-Terminal Domain (Residues 83-215) Of Pf1911 Hydrogenase From Pyrococcus Furiosus, Northeast Structural Genomics Consortium Target Pfr246a |
PDB | 1ava_B | 0 | 26 | 415 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 26 | 415 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 26 | 415 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 3bsg_A | 0 | 26 | 415 | 2 | 404 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch degradation I | RXN-1823 | EC-3.2.1.1 | α-amylase |
starch degradation I | RXN-1825 | EC-3.2.1.1 | α-amylase |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
BU103706 | 416 | 1 | 416 | 0 |
HO780661 | 404 | 13 | 416 | 0 |
HO798064 | 370 | 20 | 389 | 0 |
JG919092 | 267 | 134 | 400 | 0 |
HO798064 | 33 | 384 | 416 | 0.00001 |
Sequence Alignments (This image is cropped. Click for full image.) |
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