| Basic Information | |
|---|---|
| Species | Sorghum bicolor |
| Cazyme ID | Sb03g032830.1 |
| Family | CBM45 |
| Protein Properties | Length: 821 Molecular Weight: 92401.5 Isoelectric Point: 5.0112 |
| Chromosome | Chromosome/Scaffold: 3 Start: 61281030 End: 61295493 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| CBM45 | 241 | 319 | 5.6e-22 |
| IHWGVCKDNNMTWEIPPEPHPPTTKIFRQKALQTLLQQKADGAGNSISFSLDAEYSCLFFVLKLDEYTWLRNLENGSDF | |||
| CBM45 | 58 | 143 | 3.4e-26 |
| LHWGVSYDDEYGREWDQPPSEMRPPGSVAIKDYAIETPLEILPNSEGQLLYEVQIKFDKDIPIAAVNFVLKEEETGAWFQHKGGDF | |||
| GH13 | 455 | 740 | 3.5e-37 |
| ELSSLGFTIVWSPPPTDSVSPEGYMPRDLYNLNSRYGSMDELKELVKIFHEAGIKVLGDAVLNHRCAQFQNNNGVWNIFGGRMNWDDRAVVADDPHFQGR GNKSSGDNFHAAPNIDHSQEFVRNDLKEWLCWMRKEVGYDGWRLDFVRGFWGGYVKDYLEASEPYFAVGEYWDSLSYTYGEMDYNQDAHRQRIVDWINAT NGTAGAFDVTTKGILHAALERSEYWRLSDEKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPYGMELQGYAYILTHPGTPAVFY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 821 Download |
| MASVCISSFF GLGVLLMLQL CGETQVEGKA WVRVDAEPDA EGKCKVVVGC NVAGKWVLHW 60 GVSYDDEYGR EWDQPPSEMR PPGSVAIKDY AIETPLEILP NSEGQLLYEV QIKFDKDIPI 120 AAVNFVLKEE ETGAWFQHKG GDFRIPLNGS FNGGGKQDID IWPGDLGHAL KKSEASSSQP 180 QNTSPQDTGL SGKHISGFYE EYPILKSEYV QNLVTVTVRR DIETHKRLVE FDTDISGDVV 240 IHWGVCKDNN MTWEIPPEPH PPTTKIFRQK ALQTLLQQKA DGAGNSISFS LDAEYSCLFF 300 VLKLDEYTWL RNLENGSDFC VPLTRVGQHG STQDPDKAEE QKVEDKSSQA DGLIGDIRNL 360 VVGLSSRRGQ KAKNKVLQED ILQEIERLAA EAYSIFRSPT IDSVDDESVH LDDTLSAKPA 420 CSGTGSGFEI LCQGFNWESH KSGKWYVELG TKAKELSSLG FTIVWSPPPT DSVSPEGYMP 480 RDLYNLNSRY GSMDELKELV KIFHEAGIKV LGDAVLNHRC AQFQNNNGVW NIFGGRMNWD 540 DRAVVADDPH FQGRGNKSSG DNFHAAPNID HSQEFVRNDL KEWLCWMRKE VGYDGWRLDF 600 VRGFWGGYVK DYLEASEPYF AVGEYWDSLS YTYGEMDYNQ DAHRQRIVDW INATNGTAGA 660 FDVTTKGILH AALERSEYWR LSDEKGKPPG VLGWWPSRAV TFIENHDTGS TQGHWRFPYG 720 MELQGYAYIL THPGTPAVFY DHIFSHLQPE IAKFISIRQR LKIHCRSKIK ILKADRSLYA 780 AEIDEKLTMK IGSEHFEPNG PQNWIVAAEG QDYKIWEVSS * 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 1.0e-48 | 429 | 761 | 421 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 2.0e-134 | 429 | 817 | 406 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-158 | 430 | 769 | 343 | + 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. | ||
| PLN02361 | PLN02361 | 2.0e-169 | 426 | 817 | 398 | + alpha-amylase | ||
| PLN02784 | PLN02784 | 0 | 17 | 819 | 822 | + alpha-amylase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion 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 |
| EMBL | CBI32016.1 | 0 | 26 | 819 | 86 | 885 | unnamed protein product [Vitis vinifera] |
| GenBank | EEC71386.1 | 0 | 26 | 820 | 85 | 876 | hypothetical protein OsI_03507 [Oryza sativa Indica Group] |
| RefSeq | NP_001044062.1 | 0 | 26 | 820 | 85 | 876 | Os01g0715400 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002456247.1 | 0 | 1 | 820 | 1 | 820 | hypothetical protein SORBIDRAFT_03g032830 [Sorghum bicolor] |
| RefSeq | XP_002520134.1 | 0 | 3 | 819 | 67 | 900 | alpha-amylase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3bsg_A | 0 | 429 | 817 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1rpk_A | 0 | 429 | 817 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1p6w_A | 0 | 429 | 817 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 1ht6_A | 0 | 429 | 817 | 2 | 403 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
| PDB | 2qps_A | 0 | 429 | 817 | 2 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| 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 |
