y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_001362m |
Family | CBM45 |
Protein Properties | Length: 897 Molecular Weight: 101574 Isoelectric Point: 5.8657 |
Chromosome | Chromosome/Scaffold: 01497 Start: 148856 End: 158988 |
Description | alpha-amylase-like 3 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM45 | 120 | 203 | 7.1e-28 |
LHWGVSYLDDVGSEWDQPPKDMIPPGSIPVKDYAIETPLKKSSEGQVFHEVKINLDPKSSIAALNFVLKDEETGAWYQHRGRDF | |||
GH13 | 526 | 816 | 7.6e-38 |
KEKALEISSLGFTVIWLPPPTESVSPEGYMPKDLYNLNSRYGNIDELKDLVRSLHEVGLKILGDAVLNHRCAHYQNQNGVWNIFGGRLNWDDRAIVADDP HFQGRGNKSSGDSFHAAPNIDHSQEFVRKDLKEWLCWLRDEIGYDGWRLDFVRGFWGGYVKDYIDATEPYFAVGEYWDSLSYTYGEMDHNQDAHRQRIID WINATNGAAGAFDVTTKGILHSALERCEYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPYGKEMQGYAYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 897 Download |
MSTVAIEPLY RYSPREKPLC HCRAKILKPS SLNFSPKLLS NGITSFCKFK PHRAYTVRAS 60 STDTALLETF ESSPSFFKET FSLARTETVE GKIFIRLDKD EDQQCWQLSV GCSLPGKWIL 120 HWGVSYLDDV GSEWDQPPKD MIPPGSIPVK DYAIETPLKK SSEGQVFHEV KINLDPKSSI 180 AALNFVLKDE ETGAWYQHRG RDFKVPLVDH LLIDGNVVGA KRGFNIWPGA FLPNMLLKAE 240 ELPSKDQDSN SDSKDAKQEN KHVQGFYQEQ PITKQVVIQN SATVSVTKCF KTAKNLLYLE 300 TDLPGEVVVH WGVCRDDAKN WEISAGPYPP ETTVFKNRAL RTLLQPKDGG DGCSGLFTLG 360 KEFIGFLFVL KLNENTWLKC KENDFYIPLS SSISFPAQPG QRQFEGVPVS EKTEEANQEV 420 SQVPYTDDII NEIRNLVHDI SSEKSRQTKT KEAQESILHE IEKLAAEAYS IFRTSIPTST 480 EEAVSESEPQ ETPTKICSGT GTGFEILLQG FNWESNKSGR WYMELKEKAL EISSLGFTVI 540 WLPPPTESVS PEGYMPKDLY NLNSRYGNID ELKDLVRSLH EVGLKILGDA VLNHRCAHYQ 600 NQNGVWNIFG GRLNWDDRAI VADDPHFQGR GNKSSGDSFH AAPNIDHSQE FVRKDLKEWL 660 CWLRDEIGYD GWRLDFVRGF WGGYVKDYID ATEPYFAVGE YWDSLSYTYG EMDHNQDAHR 720 QRIIDWINAT NGAAGAFDVT TKGILHSALE RCEYWRLSDQ KGKPPGVVGW WPSRAVTFIE 780 NHDTGSTQGH WRFPYGKEMQ GYAYILTHPG TPAVFYDHIF SHYQSEIASL ISLRNRKKVQ 840 CRSTVEITKA ERDVYAAIVD EKVAMKIGPG HYEPPSESQR WVLAVEGKDY KVWEAS* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 5.0e-50 | 505 | 837 | 414 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 6.0e-137 | 505 | 894 | 407 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-162 | 506 | 845 | 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 | 9.0e-169 | 503 | 894 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 896 | 901 | + 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 | 896 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 1 | 896 | 1 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 1 | 896 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 896 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 896 | 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 | 505 | 894 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 505 | 894 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 505 | 894 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 505 | 894 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 505 | 894 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
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 |
EG631183 | 908 | 1 | 897 | 0 |
HO826981 | 407 | 491 | 897 | 0 |
ES805448 | 328 | 462 | 789 | 0 |
HO811991 | 299 | 599 | 897 | 0 |
HO826981 | 30 | 460 | 489 | 0.15 |
Sequence Alignments (This image is cropped. Click for full image.) |
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