y
Basic Information | |
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Species | Sorghum bicolor |
Cazyme ID | Sb07g023010.1 |
Family | GH13 |
Protein Properties | Length: 444 Molecular Weight: 48370.4 Isoelectric Point: 6.4465 |
Chromosome | Chromosome/Scaffold: 7 Start: 57869319 End: 57870970 |
Description | alpha-amylase-like |
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 | 44 | 357 | 3.9e-37 |
KQGGWYKFLQAQVDDIAGAGATHVWLPPPSHSVAPQGYMPGRLYDLNASRYGTEAELRSLIAAFRGKGVEAVADIVINHRCADKKDGRGVYCIFEGGGGD DGGTGTGRLNWDADMICGDDTEFSNGRGNRDTGKDFGAAPDIDHLNPRVQRELSDWLCWLSADVGFTGGWRLDFAKGYSAAVAKAYVDRTRPSFVVAEIW SSLSYDGDGKPKHNQDGDRQELVDWVNAVGGPAAAFDFTTKGVLQAAVQGELWRMRDGNGKAPGMIGWLPEKAVTFVDNHDTGSTQNSWPFPRDKVMQGY AYILTHPGIPSIFY |
Full Sequence |
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Protein Sequence Length: 444 Download |
MANHLAAGLF GLLLAVAVLC LLIGSNTARA QVLFQGFNWE SCKKQGGWYK FLQAQVDDIA 60 GAGATHVWLP PPSHSVAPQG YMPGRLYDLN ASRYGTEAEL RSLIAAFRGK GVEAVADIVI 120 NHRCADKKDG RGVYCIFEGG GGDDGGTGTG RLNWDADMIC GDDTEFSNGR GNRDTGKDFG 180 AAPDIDHLNP RVQRELSDWL CWLSADVGFT GGWRLDFAKG YSAAVAKAYV DRTRPSFVVA 240 EIWSSLSYDG DGKPKHNQDG DRQELVDWVN AVGGPAAAFD FTTKGVLQAA VQGELWRMRD 300 GNGKAPGMIG WLPEKAVTFV DNHDTGSTQN SWPFPRDKVM QGYAYILTHP GIPSIFYDHV 360 FEWNLKQEIS TLAAIRKRNG IHPGSKLSIV KAEGDVYVAM IDDKVITKIG TRYDVGSVIP 420 SGFSVAAHGD GYCIWEKRDY HYH* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-43 | 29 | 378 | 420 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02361 | PLN02361 | 9.0e-145 | 31 | 437 | 412 | + alpha-amylase | ||
PLN02784 | PLN02784 | 5.0e-150 | 31 | 437 | 408 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-157 | 32 | 387 | 359 | + 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. | ||
PLN00196 | PLN00196 | 0 | 23 | 437 | 418 | + alpha-amylase; Provisional |
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 |
GenBank | EAZ09376.1 | 0 | 24 | 437 | 20 | 426 | hypothetical protein OsI_31649 [Oryza sativa Indica Group] |
RefSeq | NP_001063368.1 | 0 | 28 | 437 | 24 | 426 | Os09g0457600 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001063369.1 | 0 | 24 | 437 | 20 | 426 | Os09g0457800 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002444507.1 | 0 | 26 | 443 | 26 | 443 | hypothetical protein SORBIDRAFT_07g023010 [Sorghum bicolor] |
RefSeq | XP_002460331.1 | 0 | 24 | 437 | 20 | 426 | hypothetical protein SORBIDRAFT_02g026610 [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 | 31 | 437 | 1 | 402 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 1ava_B | 0 | 31 | 437 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 31 | 437 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 31 | 437 | 1 | 402 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1rpk_A | 0 | 31 | 438 | 2 | 405 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
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 |