Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr7g013300.1 |
Family | GH13 |
Protein Properties | Length: 1122 Molecular Weight: 126914 Isoelectric Point: 6.7817 |
Chromosome | Chromosome/Scaffold: 7 Start: 3400170 End: 3413011 |
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 | 601 | 808 | 3.4e-25 |
ASKAADLSKCGVTAVWLPPPTESVAAQGYMPSDLYNLNSSYGSVEELKYCIEELHTHDLLALGDVVLNHRCAHKQSPNGVWNIFGGKLAWGPEAIVCDDP HFQGRGNPSSGDIFHAAPNIDHSQEFVRKDIKEWLNWLRSDIGFDGWRLDFVKRYSCSIANYDLKFDNFLFASNRGFSGTYVKEYIEASNPVFAIGEYWD SLSYEHGS |
Full Sequence |
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Protein Sequence Length: 1122 Download |
MGAAVLPDTA VLGAVLKRYP FVPRHRFTRG ISSTLSVRNR GWPSGEGLGL RSVSYSVADK 60 RIFKSAHIVF SHNNGDDMFT DIVVDQDLGK NEVLGIEDEL IAAKKSLSEA QDRQEAIEKE 120 RDQLLEELAR SEARKQEYSA AILHDKEVAI RELEAAKSLF QKNLEESVEE KFSLQSKLVL 180 AKSDAVDLAV QVEKLAEAAF QQATSHILQD AQFRISSAET TAAEAAHQIE KQIKDATEGT 240 ISSIVEKSKH AIERALAVAE EAGEHAKEAM ETFIDGTSPF TEITSVQVEN IKLQGMLSDL 300 ESQMMVARNE VARLNIELEH TRQQVKAFEQ RAIDAEKALL DLQESHRKTT LQQEEEMKSL 360 MEKMRKDVAD KTKAISKAFK TDLKNIKATI EASKEVVVSK DNAYLRRCAA LQRSLMTSED 420 ALKMWKQRAE MAEAWLMKER KLDVEDEDSI YAVNGGRIDL LTDVDSQKWK LLSDGPRRDI 480 PQWMARRIKA VIPKFPPKKT DVAEALTSKF RSLELPKADE VWSIAREKPK EGDALIEHVF 540 ERETIEKKRK ALERALQRKT IKWEKAPEQK ILEPGTGTGR EIVFQAFNWE SWRRQWYQEL 600 ASKAADLSKC GVTAVWLPPP TESVAAQGYM PSDLYNLNSS YGSVEELKYC IEELHTHDLL 660 ALGDVVLNHR CAHKQSPNGV WNIFGGKLAW GPEAIVCDDP HFQGRGNPSS GDIFHAAPNI 720 DHSQEFVRKD IKEWLNWLRS DIGFDGWRLD FVKRYSCSIA NYDLKFDNFL FASNRGFSGT 780 YVKEYIEASN PVFAIGEYWD SLSYEHGSLC YNQVTKLKHK RLKDRIAGIA QFHADFTYSC 840 DFPGILLNSG FYSRSESIGV SEFASLGVLG ITSNPIGHES MIFVLLTNYP LSNTDTNCYR 900 CRHVSVVSVS VLQRSGDVLC NIKSGKGKKE FNRNFMTNAH RQRIVNWINA TGGTSSAFDI 960 TTKGILHSAL HNEYWRMIDP QGKPTGVMGW WPSRAVTFLE NHDTGSTQGH WPFPRDKLMQ 1020 GYAYILTHPG TPVIFYDHFY DFGIHDVITE LIEARRRAGI HCRSSIKIYN ANNEGYVAQV 1080 GDSLVMKLGQ FDWNPSKENR LEGSWQKFVD KGSDYQVWLR Q* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02784 | PLN02784 | 2.0e-71 | 938 | 1118 | 182 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 7.0e-74 | 582 | 805 | 227 | + 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-75 | 579 | 837 | 265 | + alpha-amylase | ||
PLN02361 | PLN02361 | 3.0e-82 | 934 | 1118 | 187 | + alpha-amylase | ||
PLN02784 | PLN02784 | 2.0e-107 | 564 | 813 | 251 | + 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 | 1 | 813 | 1 | 791 | unnamed protein product [Vitis vinifera] |
EMBL | CBI21221.1 | 0 | 935 | 1121 | 789 | 975 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002276872.1 | 0 | 1 | 813 | 1 | 791 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002526120.1 | 0 | 135 | 813 | 136 | 788 | alpha-amylase, putative [Ricinus communis] |
RefSeq | XP_002526120.1 | 0 | 935 | 1121 | 786 | 972 | 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 | 3bsh_A | 0 | 917 | 1089 | 205 | 377 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
PDB | 3bsh_A | 0 | 580 | 803 | 1 | 211 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) Double Mutant Y105aY380A IN COMPLEX WITH INHIBITOR ACARBOSE |
PDB | 3bsg_A | 0 | 917 | 1089 | 205 | 377 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 3bsg_A | 0 | 580 | 803 | 1 | 211 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 917 | 1089 | 205 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO778903 | 515 | 89 | 603 | 0 |
HO778903 | 105 | 603 | 707 | 0 |
HO795567 | 476 | 338 | 813 | 0 |
HO795567 | 188 | 935 | 1122 | 0 |
CF210524 | 300 | 450 | 749 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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