| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | Cre08.g362450.t1.2 |
| Family | GH13 |
| Protein Properties | Length: 707 Molecular Weight: 77555.6 Isoelectric Point: 8.2967 |
| Chromosome | Chromosome/Scaffold: 8 Start: 1103176 End: 1109536 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 327 | 617 | 9.40271e-43 |
| MGRVKDISDAGFTGVWMPPPSDSVSPQGYLPRDLYSLDSAYGSEAELRELIAAFHQNNIKVIADIVVNHRCANSQGSDGKWNKFGGRLAWDASAICSNNP SFGGRGNPKQGDDYAAAPNIDHSQERIRNDIVQWMKYLRNSIGFDGWRFDFVRGYLGSYCKQYIDETVPAMAFGEYWDSCEYTDGVLNYNQDAHRQRTVN WCDSTGGTSAAFDFTTKGILQEAVGRREYWRLVDSQGRPPGVMGMWPSRAITFIDNHDTGSTLNHWPFPSRNLPEGYAYILTHPGTPCVFY | |||
| Full Sequence |
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| Protein Sequence Length: 707 Download |
| MDRSLLSRTS PRMQLGRPQQ LPPPTVPLAQ VPRLQRRCVV GSRVCQPVVA VRPGRASAGR 60 GGRLVVSSVD MSNSPLSSMD AGEGLDIMFD NNSDAECTVV TVEGKDKAHL LMSLTGGFSS 120 AGLTVISASI TSDDGRVLDV FRVQTADGKK VPEEQFPSVR EHILSVTATS SRSSMPAIYG 180 IVAAAEVERL KPLRSQSTQN DVDALELAAA EMTQAVAELV ATERDIIRMR ASNADARTLQ 240 TKEANRTEAA AGLERKMAAM QAVLAARRNL ATEPEKPKSP TEKLLETLKP PTPMRAAAGA 300 GSGSGSEILL QAFNWESHRQ KLYKQLMGRV KDISDAGFTG VWMPPPSDSV SPQGYLPRDL 360 YSLDSAYGSE AELRELIAAF HQNNIKVIAD IVVNHRCANS QGSDGKWNKF GGRLAWDASA 420 ICSNNPSFGG RGNPKQGDDY AAAPNIDHSQ ERIRNDIVQW MKYLRNSIGF DGWRFDFVRG 480 YLGSYCKQYI DETVPAMAFG EYWDSCEYTD GVLNYNQDAH RQRTVNWCDS TGGTSAAFDF 540 TTKGILQEAV GRREYWRLVD SQGRPPGVMG MWPSRAITFI DNHDTGSTLN HWPFPSRNLP 600 EGYAYILTHP GTPCVFYDHF YQEENNLRKI ILDLLKVRRR NGLNARSKVV MKKSAADVYA 660 AMIDDKVAVK LGPGDWSPNQ SGIKVNGKEL KVAASGFQFA VWEGQH* 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 3.0e-49 | 307 | 640 | 410 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 2.0e-145 | 307 | 703 | 410 | + alpha-amylase; Provisional | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-175 | 308 | 649 | 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-179 | 307 | 703 | 399 | + alpha-amylase | ||
| PLN02361 | PLN02361 | 0 | 307 | 703 | 400 | + alpha-amylase | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAS88900.1 | 0 | 228 | 703 | 8 | 502 | AAMYII [Ostreococcus tauri] |
| EMBL | CAL58037.1 | 0 | 111 | 705 | 207 | 902 | alpha amylase 1 (IC) [Ostreococcus tauri] |
| RefSeq | XP_001421556.1 | 0 | 247 | 706 | 21 | 506 | predicted protein [Ostreococcus lucimarinus CCE9901] |
| RefSeq | XP_001696014.1 | 0 | 294 | 706 | 1 | 413 | alpha-amylase [Chlamydomonas reinhardtii] |
| RefSeq | XP_002526120.1 | 0 | 275 | 702 | 543 | 969 | 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 | 1bg9_A | 0 | 307 | 703 | 1 | 401 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 1ava_B | 0 | 307 | 703 | 1 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1ava_A | 0 | 307 | 703 | 1 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 1amy_A | 0 | 307 | 703 | 1 | 401 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
| PDB | 2qpu_C | 0 | 307 | 703 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| 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 |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FC107048 | 262 | 415 | 676 | 0 |
| BQ821816 | 229 | 402 | 630 | 0 |
| HO826981 | 400 | 307 | 703 | 0 |
| HO795567 | 396 | 307 | 702 | 0 |
| EG631183 | 512 | 195 | 703 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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