y
Basic Information | |
---|---|
Species | Populus trichocarpa |
Cazyme ID | Potri.010G092900.1 |
Family | CBM45 |
Protein Properties | Length: 918 Molecular Weight: 102745 Isoelectric Point: 6.7302 |
Chromosome | Chromosome/Scaffold: 10 Start: 11582343 End: 11593518 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
CBM45 | 331 | 407 | 4.1e-23 |
VHWGVCRDDAKKWEIPAAPHPPETTVFKNKALRTVLQAKEDGNGRSGSFTLDEDLVGFLFVLKLNDSTWLNCMGNDF | |||
CBM45 | 140 | 223 | 5e-27 |
LHWGVSYLDDTGSEWDQPPENMRPPGSIPVKDYAIETPLKKASEGDKFHQVKIGIDPKSPVAALNFVLKDEETGVWYQHKGRDF | |||
GH13 | 547 | 837 | 2.2e-38 |
KQKIEEISSLGFTVVWLPPPTESVSPEGYMPKDLYNLNSRYGNIDELKDLVKRFHGKGVKVLGDAVLNHRCAHYKNGNGVWNIFGGRLNWDDRAVVADDP HFQGRGNKSSGDNFHAAPNIDHSQEFVRKDLKEWLLWLRKEIGYDGWRLDFVRGFWGGYVKDYLDASEPYFAVGEYWDSLSYTYGELDHDQDAHRQRIVD WINATSGTAGAFDVTTKGILHTTLERCEYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPSGKEMQGYAYILTHPGTPAVFY |
Full Sequence |
---|
Protein Sequence Length: 918 Download |
MSAVSVEPFL RYSRFEKPGY ARSRRKAAIT VTTAALIKSP SSFNCCCSLI PRRKLLSNAS 60 YFPFLDLHRV KTHTARASST DTALVESTND VVFKETFPLS RTEMTEGKIF VRLDQSKAKE 120 KEDQWQQLTV GCSLPGKWIL HWGVSYLDDT GSEWDQPPEN MRPPGSIPVK DYAIETPLKK 180 ASEGDKFHQV KIGIDPKSPV AALNFVLKDE ETGVWYQHKG RDFKVPLVDC LLDSGGGNVI 240 GAKGGFSMWP GAMLSNMFLK ADALASEGKD SSSRSKDPKQ ETRKVEGFYE ELPIAKFAVI 300 ENSVTVSVIK CLKTAKNLLY LVTDLPGEVV VHWGVCRDDA KKWEIPAAPH PPETTVFKNK 360 ALRTVLQAKE DGNGRSGSFT LDEDLVGFLF VLKLNDSTWL NCMGNDFYIA LPISSSIPAL 420 SGAGQSEVAP VSENTVGADQ EVSHAIYTDG IINEIRSLVS DFSSEKRQKT KTKEAQESIL 480 QEIEKLAAEA YSIFRSSIPT FLDETALESE ATEAPKICSG TGTGHEILLQ GFNWESHKLG 540 HWYMELKQKI EEISSLGFTV VWLPPPTESV SPEGYMPKDL YNLNSRYGNI DELKDLVKRF 600 HGKGVKVLGD AVLNHRCAHY KNGNGVWNIF GGRLNWDDRA VVADDPHFQG RGNKSSGDNF 660 HAAPNIDHSQ EFVRKDLKEW LLWLRKEIGY DGWRLDFVRG FWGGYVKDYL DASEPYFAVG 720 EYWDSLSYTY GELDHDQDAH RQRIVDWINA TSGTAGAFDV TTKGILHTTL ERCEYWRLSD 780 QKGKPPGVVG WWPSRAVTFI ENHDTGSTQG HWRFPSGKEM QGYAYILTHP GTPAVFYDHI 840 FSHYQSEIAA LISLRNRNKI HCRSTVKITK AERDVYAAII DEKVAVKIGP GHYEPPSGPY 900 SWSSKIEGRN YKVWEAS* 960 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-49 | 523 | 857 | 420 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 7.0e-143 | 526 | 915 | 403 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-165 | 527 | 866 | 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 | 1.0e-169 | 524 | 915 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 917 | 923 | + alpha-amylase |
Gene Ontology | |
---|---|
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 | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAX33231.1 | 0 | 1 | 917 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
EMBL | CAN69906.1 | 0 | 1 | 917 | 1 | 887 | hypothetical protein [Vitis vinifera] |
EMBL | CBI32016.1 | 0 | 1 | 917 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 917 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 917 | 1 | 900 | alpha-amylase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2qpu_C | 0 | 525 | 915 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 525 | 915 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 525 | 915 | 1 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 525 | 915 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 525 | 915 | 1 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
Metabolic Pathways | |||
---|---|---|---|
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 | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
EG631183 | 927 | 1 | 918 | 0 |
HO826981 | 405 | 514 | 918 | 0 |
HO811991 | 299 | 620 | 918 | 0 |
ES805448 | 328 | 484 | 810 | 0 |
HO826981 | 27 | 482 | 508 | 0.21 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|