| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb02g023250.1 |
| Family | GH13 |
| Protein Properties | Length: 835 Molecular Weight: 91769.3 Isoelectric Point: 5.4862 |
| Chromosome | Chromosome/Scaffold: 2 Start: 56838044 End: 56841652 |
| Description | alpha-amylase-like |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 49 | 347 | 1.5e-36 |
| SQVDDIAAAGITHVWLPPPSHSVDAQGYLPGRLYDLNVSQYGNETQLRALIAAFHGKGVKCIADIVLNHRTAESKDGRGVYCIFEGGTPDGRLDWGPHMI CRNDSYSDGTGNADTGLDYEPAPDLDHLNDVVRSDLTGWLEWLKSDAVGFDGWRLDFANGYSPAVAGGYINSTAPDVAVAEIWTDLAYEQDGRPRADQDA HRQVLADWVDAVGGPAAAFDYTTKGILQAALNYSQLSWMKDAQGRAPGLVGLRPQQAVTFVDNHDTGSKTHQLWPFPPANILQGYAYILTHPGTPCIFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 835 Download |
| MRVGTGNLIL VVILLGLSSQ AALSQILLQA FDWESWNKGG SGWYDYLQSQ VDDIAAAGIT 60 HVWLPPPSHS VDAQGYLPGR LYDLNVSQYG NETQLRALIA AFHGKGVKCI ADIVLNHRTA 120 ESKDGRGVYC IFEGGTPDGR LDWGPHMICR NDSYSDGTGN ADTGLDYEPA PDLDHLNDVV 180 RSDLTGWLEW LKSDAVGFDG WRLDFANGYS PAVAGGYINS TAPDVAVAEI WTDLAYEQDG 240 RPRADQDAHR QVLADWVDAV GGPAAAFDYT TKGILQAALN YSQLSWMKDA QGRAPGLVGL 300 RPQQAVTFVD NHDTGSKTHQ LWPFPPANIL QGYAYILTHP GTPCIFYDHF FDPSMKDQIT 360 TMMKIRTRNK IGPASKLRIL LAENDAYVAE IDGSVLTKVG PRYDVSKYVP DGFLVTTSGS 420 DFAIWENRSR RWVTPVVATV APLSALLACG AAVMLLFRRQ KRRSRQRRLP GSVDATGDHS 480 DDEEDDDDRD QADFEKGVVG PRRYHYRELA AATGNFDEEN KLGSGGFGPV YRGYLAAQDR 540 HVAVKVLSPE TSTQGRRQFE AEVRIISQLR HRNLVQLVGW CESRRNRRGG LLLVYELVAE 600 GSLDQHLYGV AERLLAWPER YRIAAGLGAA LAYLHEEWEQ CVVHGDVKPS NVMLDSSHTA 660 KLGDFGLARL LDHGVVPRTT RVVMGTMGYM DPDLVTTHKP SRASDVYSFG VVLLEVACGR 720 PATEEMPDGE TLALPEWVWE LYDRGAVLEA ADGRLDGQFD VWEMERMLVV GLWCSHPVPR 780 ERPSIVHALN VLQSRDATLP ALPTNVHRGA AAPTAGFSAY VHSMSSVGSV GEPC* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd00180 | PKc | 4.0e-46 | 522 | 715 | 196 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
| PLN02361 | PLN02361 | 4.0e-112 | 31 | 426 | 401 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 5.0e-113 | 31 | 426 | 396 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-140 | 31 | 377 | 349 | + 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 | 31 | 426 | 400 | + alpha-amylase; Provisional | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004556 | alpha-amylase activity |
| GO:0004672 | protein kinase activity |
| GO:0005509 | calcium ion binding |
| GO:0005524 | ATP binding |
| GO:0005975 | carbohydrate metabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAA33885.1 | 0 | 16 | 426 | 23 | 432 | alpha-amylase (EC 3.2.1.1) [Oryza sativa] |
| EMBL | CAA34516.1 | 0 | 16 | 426 | 17 | 426 | alpha-amylase [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001048220.1 | 0 | 16 | 426 | 23 | 432 | Os02g0765600 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002452881.1 | 0 | 8 | 427 | 8 | 427 | hypothetical protein SORBIDRAFT_04g034150 [Sorghum bicolor] |
| RefSeq | XP_002460139.1 | 0 | 1 | 834 | 1 | 834 | hypothetical protein SORBIDRAFT_02g023250 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2qpu_C | 0 | 25 | 428 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 25 | 428 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 25 | 428 | 2 | 405 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 3bsg_A | 0 | 25 | 428 | 2 | 405 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 25 | 428 | 2 | 405 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| Metabolic Pathways | |||
|---|---|---|---|
| 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 |
