Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.003G069200.1 |
Family | CBM45 |
Protein Properties | Length: 925 Molecular Weight: 104728 Isoelectric Point: 5.2489 |
Chromosome | Chromosome/Scaffold: 03 Start: 10231216 End: 10244012 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM45 | 326 | 402 | 6.6e-23 |
LHWGVCRDDLRWWEIPPTPHPPETIAFKDRALRTKLQSRDNGVGSSVQLSLGEELSGFLFVLKLNDGAWINDMGDDF | |||
CBM45 | 132 | 218 | 7.7e-28 |
LHWGVSRVDDVGSEWDQPPRDMIPPGSIPIKDYAIETPMQKSLSSAEGDALHEVKIDLKPNNDISAINFVLKDEETGAWYQYKGRDF | |||
GH13 | 555 | 843 | 7.8e-38 |
EKAAELASFGVTVIWLPPPTESVSPEGYMPKDLYNLNSRYGTVDQLKDVVKSFHEVGIKVLGDVVLNHRCAHYKNQNGIWNLFGGRLDWDDRAIVADDPH FQGRGNKSSGDNFHAAPNIDHSQEFVRKDLKEWLLWLREEIGYDGWRLDFVRGFWGGYVKDYLEATEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIVDW INATGGTAGAFDVTTKGILHSALERCEYWRLSDQKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPSGKEMQGYAYTLTHPGTPSVF |
Full Sequence |
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Protein Sequence Length: 925 Download |
MSIYTTLSFD PLFSFNHCVN REREPSIHSS RPKLFSLTSS STLTLFNSNN NCTYNYASCK 60 PHRFHTPKFE SFATNTDTLE SLQSSDVLFD RSFPINRTEL VEGKIFVRLD HGKDLGNWEL 120 TVACNLTGKW ILHWGVSRVD DVGSEWDQPP RDMIPPGSIP IKDYAIETPM QKSLSSAEGD 180 ALHEVKIDLK PNNDISAINF VLKDEETGAW YQYKGRDFKV PLVNYLKEDA NIIGPKKGFS 240 LWPGALGQIS NILLKSDATH DKVQDGNTGS RNTKVENSQL EGFYVELPIT KEISVNNSIS 300 VSIRKCSETA KNNLYLETDI PGDILLHWGV CRDDLRWWEI PPTPHPPETI AFKDRALRTK 360 LQSRDNGVGS SVQLSLGEEL SGFLFVLKLN DGAWINDMGD DFYIPLPRSS SLIIDNRENQ 420 FEGVQREVTE VTEEAGEEES ISAFTDEIIS EIRHLVTDIS SEKNRKTKSK EAQETILQEI 480 EKLAAEAYSI FRNSVPTFSE ETITESETAV ESKTVIFPEL PPQVSSGTGT GYEILCQGFN 540 WESHKSGRWY MELKEKAAEL ASFGVTVIWL PPPTESVSPE GYMPKDLYNL NSRYGTVDQL 600 KDVVKSFHEV GIKVLGDVVL NHRCAHYKNQ NGIWNLFGGR LDWDDRAIVA DDPHFQGRGN 660 KSSGDNFHAA PNIDHSQEFV RKDLKEWLLW LREEIGYDGW RLDFVRGFWG GYVKDYLEAT 720 EPYFAVGEYW DSLSYTYGEM DHNQDAHRQR IVDWINATGG TAGAFDVTTK GILHSALERC 780 EYWRLSDQKG KPPGVLGWWP SRAVTFIENH DTGSTQGHWR FPSGKEMQGY AYTLTHPGTP 840 SVFFDHLFSH YKTEISTLLS IRKRNKIQCR STVKICKAER DVYAAVIDEK VAMKIGPGQF 900 EPPSGSQKWS SVLEGRDYKI WEAS* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-48 | 533 | 864 | 416 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 2.0e-141 | 524 | 922 | 416 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-163 | 534 | 873 | 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 | 531 | 922 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 60 | 924 | 865 | + 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 | 5 | 924 | 2 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 73 | 924 | 60 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 82 | 924 | 67 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 82 | 924 | 67 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 5 | 924 | 2 | 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 | 532 | 922 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 532 | 922 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 532 | 922 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qps_A | 0 | 532 | 922 | 1 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 3bsg_A | 0 | 532 | 922 | 1 | 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 | 864 | 64 | 925 | 0 |
HO826981 | 407 | 519 | 925 | 0 |
HO782468 | 237 | 96 | 332 | 0 |
HO782468 | 243 | 333 | 575 | 0 |
HO826981 | 20 | 479 | 498 | 0.6 |
Sequence Alignments (This image is cropped. Click for full image.) |
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