Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.008G182600.3 |
Family | CBM45 |
Protein Properties | Length: 891 Molecular Weight: 100336 Isoelectric Point: 6.7065 |
Chromosome | Chromosome/Scaffold: 08 Start: 46044569 End: 46052878 |
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 | 123 | 206 | 1.5e-26 |
LHWGVSYLGDSGSEWDQPPKGMRPPGSIPIKDYAIETPLKKLSEGDIFHEVKIDFNPISEIAAIHFVLKDEETGAWYQHRGMDF | |||
GH13 | 522 | 810 | 1.50001e-40 |
KASEISSLGFTVIWLPPPTESVSPEGYMPKDLYNLNSRYGTIDELKELVKSLHEVGMKVLGDVVLNHRCAHFKNQNGVWNIFGGRLNWDDRAVVADDPHF QGRGNKSSGDNFHAAPNIDHSQEFVRKDLKEWLGWLREEIGYDGWRLDFVRGFWGGYVKDYLEASGPYFAVGEYWDSLSYTYGEMDHNQDSHRQRIVDWI NATNGTAGAFDVTTKGILHSALERCEYWRLSDQKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPGGKEMQGYAYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 891 Download |
MAAVTIDSLL QNPTLLFRPK AKVLLKPPRS LDCSRNRKLP LSRGSCLCSF NPRRTIHVVR 60 ASSSETALIG NFDISSSDDI LYKDIFPVKR IEKGKFFIRL DRSKDQHDWQ FTVGCSLPGK 120 WILHWGVSYL GDSGSEWDQP PKGMRPPGSI PIKDYAIETP LKKLSEGDIF HEVKIDFNPI 180 SEIAAIHFVL KDEETGAWYQ HRGMDFKVPL VDYLEDDGNI VGAKRGFGVW SGALQQFSNV 240 LLKSEASHAD SQNNSIESKD SKNKNRCLEG FYEEQSIVKE VSVGNLVSVA VRKSPETGKV 300 VVCLETDIPG DVVVHWGVCR DDAKIWKIPA APYPPETTVF KNKALRTLLQ PKATGNRSGA 360 LFTLDEEHFG FLFVLKLDDN TWLKFKENDF YVPLLGTSSV PGQYGQSDST SEEISSKSYT 420 DGIINEIRNL VSGLSSEKSL KTKKKEVQES ILQEIEQLAA EAYSIFRSSI TTVPDEVVSE 480 TETTKPAVKI SSGTGTGFEI LCQGFNWESH KSRRWYMELK EKASEISSLG FTVIWLPPPT 540 ESVSPEGYMP KDLYNLNSRY GTIDELKELV KSLHEVGMKV LGDVVLNHRC AHFKNQNGVW 600 NIFGGRLNWD DRAVVADDPH FQGRGNKSSG DNFHAAPNID HSQEFVRKDL KEWLGWLREE 660 IGYDGWRLDF VRGFWGGYVK DYLEASGPYF AVGEYWDSLS YTYGEMDHNQ DSHRQRIVDW 720 INATNGTAGA FDVTTKGILH SALERCEYWR LSDQKGKPPG VVGWWPSRAV TFIENHDTGS 780 TQGHWRFPGG KEMQGYAYIL THPGTPAVFY DHIFSHHRSE IASLISVRNR NGIHCRSLVK 840 IVKAERDVYA AIIDEKVAMK IGPGYYEPPS GSQRWSLALE GRDYKVWETS * 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 6.0e-51 | 499 | 830 | 418 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 8.0e-137 | 490 | 888 | 415 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-166 | 500 | 839 | 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-171 | 497 | 888 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 890 | 901 | + 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 | AAX33233.1 | 0 | 40 | 890 | 38 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CAN69906.1 | 0 | 1 | 890 | 1 | 887 | hypothetical protein [Vitis vinifera] |
EMBL | CBI32016.1 | 0 | 1 | 890 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 890 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 6 | 890 | 1 | 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 | 499 | 888 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 499 | 888 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 499 | 888 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 499 | 888 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 499 | 888 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
EG631183 | 909 | 1 | 891 | 0 |
HO826981 | 407 | 485 | 891 | 0 |
ES805448 | 383 | 456 | 838 | 0 |
DR932783 | 288 | 499 | 786 | 0 |
HO811991 | 299 | 593 | 891 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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