y
Basic Information | |
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Species | Setaria italica |
Cazyme ID | Si000308m |
Family | CBM45 |
Protein Properties | Length: 835 Molecular Weight: 92984.4 Isoelectric Point: 6.27 |
Chromosome | Chromosome/Scaffold: 5 Start: 35130029 End: 35140249 |
Description | alpha-amylase-like 3 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM45 | 304 | 382 | 6e-22 |
IHWGVCKDNSMTWEIPPEPHPPTTKIFRQKALQTLLQQKADGRGNSLSFLLDAEYSGLFFVLKLDEYTWLRNLENGSDF | |||
CBM45 | 120 | 203 | 1.7e-27 |
LHWGVSYDGEHGSEWDQPPSEMRPPGSVPIKDYAIETPLEILPNSEGRYEVQIKFDKDTPIAAINFVLKEEETGAWFQHKGRDF | |||
GH13 | 516 | 802 | 5.9e-38 |
KELASLGFTIVWSPPPTDSVSPEGYMPRDLYNLNSRYGTMDELKELVKIFHEAGIKVLGDAVLNHRCAQFQNSNGIWNIFGGRMNWDDRAVVADDPHFQG RGNKSSGDSFHAAPNIDHSQEFVRNDLKEWLCWMRKEVGYDGWRLDFVRGFWGGYVKDYLEASEPYFAVGEYWDSLSYTYGEMDYNQDAHRQRIVDWINA TNGTAGAFDVTTKGILHAALERSEYWRLSDEKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPYGMELQGYAYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 835 Download |
MSVGSGCIPA IPGAAPPARG RLLGGAFLQV AAARPRAGRC RVAQNGRVRL GGRVVARASA 60 AETPVAGAGE DAGAAFSEKF PLRRCQTVEG KAWVRVDAEP DGDGKCKVVV GCDVAGKWVL 120 HWGVSYDGEH GSEWDQPPSE MRPPGSVPIK DYAIETPLEI LPNSEGRYEV QIKFDKDTPI 180 AAINFVLKEE ETGAWFQHKG RDFRIPLSGS FDGGVPLGTN QDIGVWPGDL GHLKKHEGSN 240 AQPQETIPGG TGLSGKHISG FYQEFQIIKS EYTQNFVTVT VKRDNETHKR LVEFDTDIPG 300 EVVIHWGVCK DNSMTWEIPP EPHPPTTKIF RQKALQTLLQ QKADGRGNSL SFLLDAEYSG 360 LFFVLKLDEY TWLRNLENGS DFFISLTRAE QRGSTQDVDK VEPQKVDDKS SQADGIISDI 420 RNLVVGLSSR RGQRAKNKVL QEDILQEIER LAAEAYSIFR SPTIDSVEAS VDLDDPSIAK 480 PACSGTGSGY EILCQGFNWE SHKSGKWYVE LGTKAKELAS LGFTIVWSPP PTDSVSPEGY 540 MPRDLYNLNS RYGTMDELKE LVKIFHEAGI KVLGDAVLNH RCAQFQNSNG IWNIFGGRMN 600 WDDRAVVADD PHFQGRGNKS SGDSFHAAPN IDHSQEFVRN DLKEWLCWMR KEVGYDGWRL 660 DFVRGFWGGY VKDYLEASEP YFAVGEYWDS LSYTYGEMDY NQDAHRQRIV DWINATNGTA 720 GAFDVTTKGI LHAALERSEY WRLSDEKGKP PGVLGWWPSR AVTFIENHDT GSTQGHWRFP 780 YGMELQGYAY ILTHPGTPAV FYDHIFSHLQ PEIAKFINIR SRQKIHCRSK VKCK* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 3.0e-49 | 491 | 822 | 418 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 3.0e-119 | 491 | 832 | 355 | + alpha-amylase; Provisional | ||
PLN02361 | PLN02361 | 4.0e-152 | 488 | 832 | 351 | + alpha-amylase | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 5.0e-158 | 492 | 831 | 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. | ||
PLN02784 | PLN02784 | 0 | 62 | 832 | 786 | + alpha-amylase |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
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 | AAX33231.1 | 0 | 42 | 832 | 43 | 851 | plastid alpha-amylase [Malus x domestica] |
EMBL | CBI32016.1 | 0 | 70 | 832 | 68 | 835 | unnamed protein product [Vitis vinifera] |
GenBank | EEC71386.1 | 0 | 1 | 833 | 1 | 827 | hypothetical protein OsI_03507 [Oryza sativa Indica Group] |
RefSeq | NP_001044062.1 | 0 | 1 | 833 | 1 | 827 | Os01g0715400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002456247.1 | 0 | 88 | 832 | 26 | 770 | hypothetical protein SORBIDRAFT_03g032830 [Sorghum bicolor] |
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 | 490 | 832 | 1 | 355 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 2qps_A | 0 | 490 | 832 | 1 | 355 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1rpk_A | 0 | 490 | 833 | 1 | 356 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1p6w_A | 0 | 490 | 833 | 1 | 356 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |
PDB | 1ht6_A | 0 | 490 | 833 | 1 | 356 | 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 |
EG631183 | 789 | 62 | 832 | 0 |
HO826981 | 354 | 479 | 832 | 0 |
DV475507 | 279 | 502 | 780 | 0 |
DR932783 | 288 | 491 | 778 | 0 |
GO859052 | 314 | 400 | 713 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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