y
Basic Information | |
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Species | Vitis vinifera |
Cazyme ID | GSVIVT01032922001 |
Family | GH13 |
Protein Properties | Length: 976 Molecular Weight: 110139 Isoelectric Point: 5.6917 |
Chromosome | Chromosome/Scaffold: 14 Start: 24159695 End: 24204470 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 607 | 890 | 2e-39 |
LSQCGITAVWLPPPTESVAPQGYMPSDLYNLNSAYGTMEELKHCIDEMHTQDLLALGDVVLNHRCAHKQSPNGVWNIFGGKLAWGPEAIVCDDPNFQGRG NPSSGDIFHAAPNIDHSQDFVRRDIKEWLNWLRNDIGFDGWRLDFVRGFSGTYVKEYIEVSNPAFAIGEYWDSLAYEGGDLCYNQDAHRQRIINWINATD GTSSAFDVTTKGILHYALHNQYWRLIDPQGKPTGVVGWWPSRAVTFLENHDTGSTQGHWPFPRDKLTQGYAYILTHPGTPVVFY |
Full Sequence |
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Protein Sequence Length: 976 Download |
MGAILLPDAA LGFLPRHSVV SSGKHHSHVS NSCLKSHPII YRNTGSRKRK LLYTNNWLYK 60 SRSVVFSSRA DHSETFSDAD GGDSYLLEGS EALEIDEDEL VAARKALTEA CARQEAIEKE 120 RDRLMEELVQ SEAKQKEYVA TLMHDKELAI AELQAVKSLF HQKLQDTVEE KSTLESKLVL 180 AKQDAVELAV QVEKLAEIAI HQATAHILED AQLRVSAAET SAAQAVYQIE DQIRNTAERT 240 ILAVVEQSKI AIDKALVVAE RAGDYATKSV AAFTDATSPA DEIAAIQSQN IELQNATNNL 300 ESQLLLTRSE IDKLKLELEQ AHAKANASEL RANAAEKALL EFQESMKEQN LQQQEEMKRL 360 LEKVKKDAAE KKKAASKAFK LELESIKAAI EAAKETAHSK DEAYSRRCEA LHRSLRASEA 420 ALAMWRQRAE MAESLLLKEK PFSEGDEDAI FVVNGGRIDL LTDDDSQKLK LLSDGPRREL 480 PEWMARSIRT ICPKFPPRKV DASEAMKSKF ISLDLPKPDE VWSIATEKPK EGDTLIEHVI 540 EKEIIEKKRK ALERALHRKT IQWQQTPEDT QLEPGTGTGR EIVFQGFNWE SWRRQWYLEL 600 APKAADLSQC GITAVWLPPP TESVAPQGYM PSDLYNLNSA YGTMEELKHC IDEMHTQDLL 660 ALGDVVLNHR CAHKQSPNGV WNIFGGKLAW GPEAIVCDDP NFQGRGNPSS GDIFHAAPNI 720 DHSQDFVRRD IKEWLNWLRN DIGFDGWRLD FVRGFSGTYV KEYIEVSNPA FAIGEYWDSL 780 AYEGGDLCYN QDAHRQRIIN WINATDGTSS AFDVTTKGIL HYALHNQYWR LIDPQGKPTG 840 VVGWWPSRAV TFLENHDTGS TQGHWPFPRD KLTQGYAYIL THPGTPVVFY DHFYDFGLRD 900 VITELIEARR RAGIHCRSSV KIYHANNEGY VARIEDALVM KIGHFDWNPS KENDLDGSWQ 960 KFVDKGSEYQ LWLRQ* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-50 | 581 | 911 | 419 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 2.0e-144 | 581 | 943 | 376 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-165 | 582 | 920 | 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 | 3.0e-177 | 579 | 972 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 569 | 972 | 408 | + 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 |
EMBL | CBI21221.1 | 0 | 1 | 975 | 1 | 975 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001782830.1 | 0 | 583 | 974 | 14 | 404 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002276872.1 | 0 | 1 | 968 | 1 | 968 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324108.1 | 0 | 584 | 975 | 10 | 401 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002526120.1 | 0 | 1 | 975 | 1 | 972 | 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 | 3bsg_A | 0 | 581 | 943 | 2 | 377 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 580 | 943 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1rpk_A | 0 | 580 | 943 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1p6w_A | 0 | 580 | 943 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1ht6_A | 0 | 580 | 943 | 1 | 377 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
Metabolic Pathways | |||
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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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO795567 | 639 | 338 | 976 | 0 |
HO785297 | 258 | 586 | 843 | 0 |
HO785297 | 103 | 863 | 965 | 0 |
HO785297 | 26 | 844 | 869 | 0 |
HO785297 | 55 | 530 | 584 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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