Basic Information | |
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Species | Carica papaya |
Cazyme ID | evm.model.supercontig_5.271 |
Family | CBM45 |
Protein Properties | Length: 752 Molecular Weight: 85002 Isoelectric Point: 6.8241 |
Chromosome | Chromosome/Scaffold: 5 Start: 2400904 End: 2412549 |
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 | 119 | 202 | 2.3e-29 |
LHWGVSYIDDMGSEWDQPPKDMRPPGSIPIKDYAIETPLKKSSEGDLFHEVKIDLDMKRSISAINFVLKDEETGAWYQHRGRDF | |||
GH13 | 357 | 671 | 3.9e-39 |
EKAEEIASLGFTVIWLPPPTESVSPEGYMPKDLYNLDSRYGTMDELKDTVKRFHEVGLRVLGDVVLNHRCAHYQNQNGVWDILTIVILYMVSNSFPKAYI SFGLFSHLVIQATLVRSSANKIKHLALGRGNKSSGDNFHAAPNIDHSQEFVRKDIKEWLCWLRKEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEF WDSLSYTYGEMDHNQDAHRQRIIDWINATNGTAGAFDVTTKGILHSALERCEYWRLSDQNGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGKEMQG YAYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 752 Download |
MSTVTIDPLL HHCRRESPGI RLKTKLLKLS SLDYSSKLIF NGCSSSSNLF SFKPKRLLSI 60 RAASTSVASF QSTDIFFKET FPLKRTETVE GKIFVRLDQP NGQDWQLSVG CSLPGKWILH 120 WGVSYIDDMG SEWDQPPKDM RPPGSIPIKD YAIETPLKKS SEGDLFHEVK IDLDMKRSIS 180 AINFVLKDEE TGAWYQHRGR DFRVPLVNYL QDGGNVVGAK RGFSIWPGSF LAQSEAADLS 240 GNIEEVDQEV SHAAYTEGII NEIRNLVSDI SLEKGQRTKK KAVNESILQE IEKLAAEAYS 300 IFRSSVPTFP EEIVSESDVK QPPTKICSGT GTGFEILCQG FNWESHKAGR WYMELKEKAE 360 EIASLGFTVI WLPPPTESVS PEGYMPKDLY NLDSRYGTMD ELKDTVKRFH EVGLRVLGDV 420 VLNHRCAHYQ NQNGVWDILT IVILYMVSNS FPKAYISFGL FSHLVIQATL VRSSANKIKH 480 LALGRGNKSS GDNFHAAPNI DHSQEFVRKD IKEWLCWLRK EIGYDGWRLD FVRGFWGGYV 540 KDYLDASEPY FAVGEFWDSL SYTYGEMDHN QDAHRQRIID WINATNGTAG AFDVTTKGIL 600 HSALERCEYW RLSDQNGKPP GVVGWWPSRA VTFIENHDTG STQGHWRFPG GKEMQGYAYI 660 LTHPGTPAVF YDHIFSHYRS EIATLISIRN RNKINCRSTV KITKAERDVY AAIIDEKVAV 720 KIGPGYYEPS SGPQRWSSAL EGRDYNVWEA S* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02784 | PLN02784 | 2.0e-80 | 1 | 229 | 232 | + alpha-amylase | ||
PLN00196 | PLN00196 | 8.0e-132 | 335 | 749 | 422 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-151 | 336 | 700 | 368 | + 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 | 7.0e-161 | 333 | 749 | 422 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 77 | 751 | 677 | + 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 | 251 | 1 | 258 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33231.1 | 0 | 77 | 751 | 274 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 1 | 241 | 1 | 250 | plastid alpha-amylase [Actinidia chinensis] |
GenBank | AAX33233.1 | 0 | 107 | 751 | 300 | 895 | plastid alpha-amylase [Actinidia chinensis] |
RefSeq | XP_002520134.1 | 0 | 77 | 751 | 270 | 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 | 335 | 749 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 335 | 749 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 335 | 749 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 335 | 749 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 335 | 749 | 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 | 678 | 77 | 752 | 0 |
EG631183 | 261 | 1 | 251 | 0 |
HO826981 | 432 | 321 | 752 | 0 |
ES805448 | 353 | 292 | 644 | 0 |
HO826981 | 33 | 290 | 322 | 0.013 |
Sequence Alignments (This image is cropped. Click for full image.) |
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