| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20003157m |
| Family | GH13 |
| Protein Properties | Length: 705 Molecular Weight: 76778.4 Isoelectric Point: 7.4949 |
| Chromosome | Chromosome/Scaffold: 21 Start: 2043066 End: 2050046 |
| Description | alpha-amylase-like 3 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 329 | 616 | 1.3999e-42 |
| VKDISDAGFTAVWMPPPSDSVSPQGYLPRDLYSLDSAYGSEGELRDLIASFHQHNIKVIADIVVNHRCANSQGSDGKWNKFGGRLAWDASAICSNNPAFG GRGNPKQGDDYAAAPNIDHSQERIRNDIINWMKYLRNSIGFDGWRFDFVRGYLGSYCKTYIDETVPAMAFGEYWDSCEYTDGVLNYNQDAHRQRTVNWCD STGGTSAAFDFTTKGILQEAVGRREYWRLVDSQGRPPGVMGMWPSRAITFIDNHDTGSTLNHWPFPSRNLPEGYAYILTHPGTPCVFY | |||
| Full Sequence |
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| Protein Sequence Length: 705 Download |
| MDRSLLSRTS PRMQLGRSQQ LPQSCLPPAQ VRPLPRRCAG SRPCQPAAAV RQERLSSGRG 60 GLLVASAVDM STSPISSIDA GEGLDILFDN SSDSECTVVT VEGKDKAHLL ISLTGGFSSC 120 GLSVISASIT SDDGRVLDVF RVQTADGKKV PEDQFSLVKD HILSVTSSTS RSSMPAIYGI 180 VAAAEVERLK PLKGQAAQNE VDSLELAAAE MAAAAAELVA TEREIIELRA SNAELRLVQA 240 KEAQRTEAAA GLERKMAAMQ AVLAARRNLA AVPEKQKSQA EKLLDTLKPP APTRAAAGAG 300 SGSGYEILLQ AFNWESHRQR LYRQLSGRVK DISDAGFTAV WMPPPSDSVS PQGYLPRDLY 360 SLDSAYGSEG ELRDLIASFH QHNIKVIADI VVNHRCANSQ GSDGKWNKFG GRLAWDASAI 420 CSNNPAFGGR GNPKQGDDYA AAPNIDHSQE RIRNDIINWM KYLRNSIGFD GWRFDFVRGY 480 LGSYCKTYID ETVPAMAFGE YWDSCEYTDG VLNYNQDAHR QRTVNWCDST GGTSAAFDFT 540 TKGILQEAVG RREYWRLVDS QGRPPGVMGM WPSRAITFID NHDTGSTLNH WPFPSRNLPE 600 GYAYILTHPG TPCVFYDHFY QEDGGLRKCI LELLGVRKRN GVNARSKVVV KKSAADVYAA 660 VIDDKVAVKI GPGDWSPNHA GVRTNGKDMK MASSGYQFAV WEAQ* 720 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK09441 | PRK09441 | 1.0e-48 | 306 | 639 | 412 | + cytoplasmic alpha-amylase; Reviewed | ||
| PLN00196 | PLN00196 | 8.0e-138 | 306 | 702 | 413 | + alpha-amylase; Provisional | ||
| PLN02784 | PLN02784 | 4.0e-170 | 305 | 703 | 400 | + alpha-amylase | ||
| cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-171 | 307 | 643 | 340 | + 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 | 0 | 306 | 702 | 400 | + alpha-amylase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0004556 | alpha-amylase activity |
| GO:0005509 | calcium ion binding |
| GO:0005975 | carbohydrate metabolic process |
| GO:0043169 | cation binding |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAX33231.1 | 0 | 196 | 703 | 405 | 900 | plastid alpha-amylase [Malus x domestica] |
| EMBL | CAL58037.1 | 0 | 110 | 702 | 207 | 900 | alpha amylase 1 (IC) [Ostreococcus tauri] |
| RefSeq | XP_001421556.1 | 0 | 246 | 702 | 21 | 503 | predicted protein [Ostreococcus lucimarinus CCE9901] |
| RefSeq | XP_001696014.1 | 0 | 306 | 704 | 14 | 412 | alpha-amylase [Chlamydomonas reinhardtii] |
| RefSeq | XP_002526120.1 | 0 | 274 | 704 | 543 | 972 | 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 | 2qpu_C | 0 | 305 | 672 | 1 | 378 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_B | 0 | 305 | 672 | 1 | 378 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 2qpu_A | 0 | 305 | 672 | 1 | 378 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
| PDB | 3bsg_A | 0 | 305 | 671 | 1 | 377 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
| PDB | 2qps_A | 0 | 305 | 671 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FC107048 | 262 | 414 | 675 | 0 |
| BQ821816 | 228 | 401 | 628 | 0 |
| HO795567 | 400 | 306 | 705 | 0 |
| HO826981 | 403 | 305 | 705 | 0 |
| BQ819393 | 205 | 355 | 559 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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