y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.007G082900.1 |
Family | GH13 |
Protein Properties | Length: 1003 Molecular Weight: 113848 Isoelectric Point: 6.2616 |
Chromosome | Chromosome/Scaffold: 07 Start: 5919098 End: 5928342 |
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 |
GH13 | 634 | 917 | 1.2e-36 |
LSHSGITAVWLPPPTQSVAPQGYMPSDLYNLNSSYGSVEDLKSCIEEMHSQELLALGDIVLNHRCAHKQSPNGVWNIFGGKLAWGPEAIVCDDPNFQGRG NPSSGDIFHAAPNVDHSQHFVRKDVKEWLYWLRNDIGYDGWRLDFVRGFSGTFVKEYIEASNPAFAIGEYWDSMAYEHGNLCYNQDAHRQRIVNWINATG GTSSAFDVTTKGILHSALHDQYWRLIDPQGKPTGVMGWWPSRACTFLENHDTGSTQGHWPFPRDKLTQGYAYILTHPGTPVIFY |
Full Sequence |
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Protein Sequence Length: 1003 Download |
MLVLRSLLIC FFWKQLSGQC LLLLLLLFNY NAEESKMGVF VLPSSAFGVL LPHFPVVSLG 60 TPRGQFHLVL GGSSNRKRKN LLTGNWQCRP RIVVASNRDD SKDNVTDDED GSLLGSYEML 120 EMKEDELVEA RKALSEVKAR QAALEKERDQ LLEDFASSEA KQKEYVASVL HDKELAVSEL 180 ESTKSLFHQK LQESVKEKFA LESKLVLARQ DAVELAVQVE KLAEVAFRQA TSHILEDAKL 240 RVSAAETLAA ESAFQIDEQI RKSTEGTIFS IIVESKDAIN KALDVAENAI DEATQAVAVF 300 TDAVNPIDVI ASAQSENIKL QGAVSDLEAQ LLVSESELDR LKLELQQAQV QANAAELRSS 360 NAEKALLEFQ ELSRKKALEQ EEEIRSLLEK IKKEAVERKK VLSKAFKAEL ESIKAAVDAS 420 KEITCSRENA YMRRCEALQR SLRTSESALK LWRQRAEMAQ SLLLKERSEK EDDEDVIYIA 480 NGGRIDLLTD DDSQKWKLLS YGPRKEIPQW MARRIRSIRP KFPPRKTDIS KALNSNFKSL 540 ELPKLDEVWS IAQEKLREGD MLTEHVIEKE VIEKKRKALE RALQRKTVKW KRIPEETKIE 600 PGTGTGREIV FQGFNWESWR RQWYQELAFK AADLSHSGIT AVWLPPPTQS VAPQGYMPSD 660 LYNLNSSYGS VEDLKSCIEE MHSQELLALG DIVLNHRCAH KQSPNGVWNI FGGKLAWGPE 720 AIVCDDPNFQ GRGNPSSGDI FHAAPNVDHS QHFVRKDVKE WLYWLRNDIG YDGWRLDFVR 780 GFSGTFVKEY IEASNPAFAI GEYWDSMAYE HGNLCYNQDA HRQRIVNWIN ATGGTSSAFD 840 VTTKGILHSA LHDQYWRLID PQGKPTGVMG WWPSRACTFL ENHDTGSTQG HWPFPRDKLT 900 QGYAYILTHP GTPVIFYDHF YEFGIRDVLT ELIEARRRAG IHCRSSVKIY HANTEGYVAQ 960 VSNMLVIKLG HFDWNPSKEN QLDGSWQKFI DKGADYQIWL RQ* 1020 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 2.0e-47 | 608 | 938 | 419 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 5.0e-142 | 608 | 970 | 376 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 4.0e-163 | 609 | 947 | 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 | 4.0e-178 | 606 | 999 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 598 | 999 | 406 | + 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 | 37 | 1002 | 1 | 975 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001782830.1 | 0 | 610 | 1001 | 14 | 404 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_002276872.1 | 0 | 37 | 995 | 1 | 968 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324108.1 | 0 | 611 | 1002 | 10 | 401 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002526120.1 | 0 | 37 | 1002 | 1 | 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 | 3bsg_A | 0 | 607 | 970 | 1 | 377 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 607 | 970 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1rpk_A | 0 | 607 | 970 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1p6w_A | 0 | 607 | 970 | 1 | 377 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1ht6_A | 0 | 607 | 970 | 1 | 377 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO795567 | 639 | 365 | 1003 | 0 |
HO778903 | 507 | 124 | 630 | 0 |
HO778903 | 106 | 629 | 734 | 0 |
HO785297 | 258 | 613 | 870 | 0 |
HO785297 | 103 | 890 | 992 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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