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Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.285330.1 |
Family | CBM45 |
Protein Properties | Length: 901 Molecular Weight: 101327 Isoelectric Point: 7.2853 |
Chromosome | Chromosome/Scaffold: 02653 Start: 1739563 End: 1748339 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM45 | 312 | 388 | 1.7e-22 |
VHWGACRDDTKKWEIPAAPHPPETTVFKNKALRTLLQPKEGGKGCSGVFTIEEDFGGFLFVLKQKENSWLNYKGDDF | |||
CBM45 | 120 | 205 | 1.6e-27 |
LHWGVSLIDDSGSEWDQPPKEMIPPGSITIKDYAIETPLKKSSSSSSGDVHEVKIDLAPDKTIAAINFVLKDEETGIWYQHKGRDF | |||
GH13 | 530 | 819 | 5.4e-38 |
EKAAELSSLGFTVLWLPPPTESVSPEGYMPKDLYNLNSRYGNIDELKDVVKTFHDVGIKVLGDAVLNHRCAHFKNQNGIWNIFGGRLNWDDRAVVSDDPH FQGRGNKSSGDNFHAAPNIDHSQDFVRNDIKEWLLWLRKEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIVDW INATNGTAGAFDVTTKGILHSALDRCEYWRLSDEKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGKEMQGYAYLLTHPGTPSVFY |
Full Sequence |
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Protein Sequence Length: 901 Download |
MSSIALDPLL YHCAKGKHRF HHRPRFNMLR PCSFTYCPNK LLCHGRKSFV HYNSYRPPTI 60 KATTTNAPTF QSTDVLFNET FPLKRNEKLE GRISVRLAQG KDHNNWELTV GCNLAGKWIL 120 HWGVSLIDDS GSEWDQPPKE MIPPGSITIK DYAIETPLKK SSSSSSGDVH EVKIDLAPDK 180 TIAAINFVLK DEETGIWYQH KGRDFKVPLL DYCGEDGNKV GTKKGLGLWP GALGQLSNLL 240 VKAETNSKDQ GSSSESGDTK EEKKSLEGFY KELPIVKEIA VDNSISVSVR KCSETTKYLL 300 YLESDLPGDV IVHWGACRDD TKKWEIPAAP HPPETTVFKN KALRTLLQPK EGGKGCSGVF 360 TIEEDFGGFL FVLKQKENSW LNYKGDDFYI PFPSSGNLSN QQRKSKLKDT RASKISGEES 420 EGVSVTAYTD GIIKEIRNLV TDISSQKTKK KKTKEAQESI LQEIEKLAAE AYSIFRSSAP 480 TFTEEIIETP KPVEPPVRIS SGTGSGFEIL CQGFNWESHK SGRWYMELKE KAAELSSLGF 540 TVLWLPPPTE SVSPEGYMPK DLYNLNSRYG NIDELKDVVK TFHDVGIKVL GDAVLNHRCA 600 HFKNQNGIWN IFGGRLNWDD RAVVSDDPHF QGRGNKSSGD NFHAAPNIDH SQDFVRNDIK 660 EWLLWLRKEI GYDGWRLDFV RGFWGGYVKD YLDASEPYFA VGEYWDSLSY TYGEMDHNQD 720 AHRQRIVDWI NATNGTAGAF DVTTKGILHS ALDRCEYWRL SDEKGKPPGV VGWWPSRAVT 780 FIENHDTGST QGHWRFPGGK EMQGYAYLLT HPGTPSVFYD HIFSHYKSEI AALISLRKRN 840 KVNCRSVVKI VKAERDVYAA IIDETVAVKI GPGNFEPPSG SNGWSLVIEG KDYKVWEVSK 900 * 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 8.0e-49 | 508 | 839 | 417 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 1.0e-137 | 499 | 897 | 416 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-164 | 509 | 848 | 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 | 4.0e-167 | 505 | 897 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 899 | 904 | + alpha-amylase |
Gene Ontology | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAX33231.1 | 0 | 1 | 899 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 1 | 899 | 1 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 1 | 899 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 899 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 899 | 1 | 900 | alpha-amylase, putative [Ricinus communis] |
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 | 2qpu_C | 0 | 508 | 897 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 508 | 897 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 508 | 897 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qps_A | 0 | 508 | 897 | 2 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 3bsg_A | 0 | 508 | 897 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 908 | 1 | 899 | 0 |
HO826981 | 406 | 494 | 899 | 0 |
ES805448 | 328 | 465 | 792 | 0 |
DR932783 | 288 | 508 | 795 | 0 |
HO826981 | 30 | 463 | 492 | 0.007 |
Sequence Alignments (This image is cropped. Click for full image.) |
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