Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s342_20V6.1 |
Family | GH13 |
Protein Properties | Length: 957 Molecular Weight: 105356 Isoelectric Point: 6.5638 |
Chromosome | Chromosome/Scaffold: 342 Start: 237658 End: 244337 |
Description | alpha-amylase-like 3 |
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 | 587 | 872 | 3.5e-39 |
SDLAKCGITTIWLPPPTQSVAPQGYMPGDLYNLNSAYGGSEELKLCINEMHKHKILVLGDVVLNHRCAQKQSPNGVWNIFGGKLAWGPEAIVGDDPNFQG RGNPKSGDFFHAAPNVDHSQKFVRKDIMEWMQWLRTEFGFDGWRLDFVRGFWGGYVKEYIEATKPAFAIGEYWDSLSYEGGQVSYNQDAHRQRIVNWINA TGGTSSAFDVTTKGILHSALHGEFWRLIDPQGKPPGVMGWWPSRAVTFLENHDTGSTQGHWPFPRDKLMMGYAYILTHPGTPVIFH |
Full Sequence |
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Protein Sequence Length: 957 Download |
MDTILTRSLA GVSGHLLPIG RGEFQSTSPS IHLISSYHCA GSNNNNSTIK TPFLGERVLV 60 SRNVNTTKAL RRIWHGRVFV SVLKGENNNG SRGFQIPDDV ESLKVALAAA EARADAAKKA 120 EKQALEALTA MEGKSSDTVK TSRNMKQIKL KGGNDDADGI SLAVQVEKIS EAAIQKATAR 180 ITEDATLKVA AAETAAAEAV LQLEERLQRA VDEAASAVAG ETQVAIDEAR AAAKVAKAQA 240 AKSEALLNEQ VNVLNELAEI EAKMLVLEEA LLAAGRQLQI ANGETERVRI ELDAVQSFIK 300 TATARAEAAE KTIIEVQKAA SKAADEREAS ALTAIDAVKK AAKARQVADK VAFEAEADAL 360 RSANDASHKA SEARRLVIKS RCESLEKSLV AAEGAAAAWR NRALTAEELL RQSRINGVEI 420 DSSSPVPDLL PPNIGRLEML PGSDAKIKDL LENGPRRETP DWMKRRLQTG QQNLPPMQPT 480 SITADIDAAI PLELPTPEDV WDVAKSKVKE DDKYTVRAAE KEALDLQRNA LERALQTKSL 540 RTLVRYPEES ESKTESGTGS GREIVFQGFN WESWRRQWWL EMSAKASDLA KCGITTIWLP 600 PPTQSVAPQG YMPGDLYNLN SAYGGSEELK LCINEMHKHK ILVLGDVVLN HRCAQKQSPN 660 GVWNIFGGKL AWGPEAIVGD DPNFQGRGNP KSGDFFHAAP NVDHSQKFVR KDIMEWMQWL 720 RTEFGFDGWR LDFVRGFWGG YVKEYIEATK PAFAIGEYWD SLSYEGGQVS YNQDAHRQRI 780 VNWINATGGT SSAFDVTTKG ILHSALHGEF WRLIDPQGKP PGVMGWWPSR AVTFLENHDT 840 GSTQGHWPFP RDKLMMGYAY ILTHPGTPVI FHDHFYDFGL HDQIAELIAV RTRTGVHCRS 900 PVKIFQANFE GYAAQIGENL VMKIGHLDWN PSKQNNLPGS WDRCVDKGEY QLWERI* 960 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 4.0e-44 | 563 | 891 | 418 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 2.0e-148 | 563 | 956 | 413 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 1.0e-169 | 564 | 902 | 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 | 2.0e-178 | 562 | 955 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 562 | 954 | 395 | + 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 |
EMBL | CBI21221.1 | 0 | 120 | 955 | 151 | 974 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001768202.1 | 0 | 566 | 955 | 1 | 390 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001782830.1 | 0 | 565 | 956 | 14 | 405 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002276872.1 | 0 | 120 | 948 | 151 | 966 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002526120.1 | 0 | 158 | 955 | 185 | 971 | 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 | 3bsg_A | 0 | 562 | 925 | 1 | 377 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 562 | 955 | 1 | 404 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1rpk_A | 0 | 562 | 925 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1p6w_A | 0 | 562 | 925 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1ht6_A | 0 | 562 | 925 | 1 | 377 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
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 |
HO795567 | 640 | 317 | 955 | 0 |
FC346731 | 267 | 575 | 841 | 0 |
FC326055 | 256 | 702 | 957 | 0 |
HO785297 | 258 | 568 | 825 | 0 |
HO785297 | 103 | 845 | 947 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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