Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s223_59V6.1 |
Family | GH13 |
Protein Properties | Length: 545 Molecular Weight: 60865.2 Isoelectric Point: 6.2044 |
Chromosome | Chromosome/Scaffold: 223 Start: 359808 End: 363241 |
Description | alpha-amylase-like |
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 | 169 | 460 | 8.2e-36 |
DLAAAGITDVWFPPSSHSVSPQGYMPGRLYDLNDCKYGNEEKLRETIEKFHRVGVRCIADIVVNHRCGEEQDERGEWVIFEGGTPDDALDWGPWAIVGDD YPYGNGTGAPDTGDDFEAAPDIDHTNDIVQSDLIVWMNWMKFKIGFDGWRFDFAKGYGGYFVGRYIRKTEPQFAVGEFWTSLNYGHDGLEYNQDSHRQQL VDWIHATKERSTAFDFTTKGILQEAVKGQLWRLRDPNSKPPGLIGYWPSKAVTFLDNHDTGSTQGHWPFPGEHIMQGYAYILTHPGNPCIFY |
Full Sequence |
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Protein Sequence Length: 545 Download |
MASITNQGAQ ASGLRECSIS NSMRSSIGHK AMNVCMTPST SSASSTFFSS KRLHGTHSTP 60 RRINLSAGSA SIRSSIEAPK AAKEAVENVK NAPNATMEAV EGAIKAVEGT AEAVTDAAKP 120 QLKRSRSHHK ARGGNIKADP LRVIMFQGFN WESWKSSCWY DVMGETAEDL AAAGITDVWF 180 PPSSHSVSPQ GYMPGRLYDL NDCKYGNEEK LRETIEKFHR VGVRCIADIV VNHRCGEEQD 240 ERGEWVIFEG GTPDDALDWG PWAIVGDDYP YGNGTGAPDT GDDFEAAPDI DHTNDIVQSD 300 LIVWMNWMKF KIGFDGWRFD FAKGYGGYFV GRYIRKTEPQ FAVGEFWTSL NYGHDGLEYN 360 QDSHRQQLVD WIHATKERST AFDFTTKGIL QEAVKGQLWR LRDPNSKPPG LIGYWPSKAV 420 TFLDNHDTGS TQGHWPFPGE HIMQGYAYIL THPGNPCIFY DHFYDWGLKE EIKTLIDVRK 480 RNDINAKSKV HICCAEHDLY VAKIDDRVIL KMGPRYDIGD LAPNCDEYKI AAVGKDYCVW 540 EKCT* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-43 | 144 | 481 | 417 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN02784 | PLN02784 | 6.0e-153 | 144 | 542 | 400 | + alpha-amylase | ||
PLN02361 | PLN02361 | 2.0e-161 | 142 | 542 | 405 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-174 | 144 | 490 | 350 | + 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. | ||
PLN00196 | PLN00196 | 0 | 144 | 542 | 404 | + alpha-amylase; Provisional |
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 | ABK24434.1 | 0 | 114 | 542 | 16 | 443 | unknown [Picea sitchensis] |
EMBL | CAX51374.1 | 0 | 144 | 543 | 26 | 427 | alpha-amylase [Hordeum vulgare subsp. vulgare] |
RefSeq | XP_001754460.1 | 0 | 148 | 542 | 1 | 395 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001777583.1 | 0 | 141 | 544 | 9 | 412 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002282184.1 | 0 | 144 | 542 | 25 | 424 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 1bg9_A | 0 | 144 | 543 | 2 | 403 | B Chain B, Crystal Structure Of P110beta In Complex With Icsh2 Of P85beta And The Drug Gdc-0941 |
PDB | 1ava_B | 0 | 144 | 543 | 2 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1ava_A | 0 | 144 | 543 | 2 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 1amy_A | 0 | 144 | 543 | 2 | 403 | A Chain A, Amy2BASI PROTEIN-Protein Complex From Barley Seed |
PDB | 2qpu_C | 0 | 144 | 542 | 3 | 404 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
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 |
HO476908 | 488 | 58 | 544 | 0 |
FC414887 | 258 | 151 | 408 | 0 |
HO409542 | 405 | 139 | 542 | 0 |
FC451168 | 261 | 56 | 316 | 0 |
HO420508 | 401 | 143 | 542 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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