Basic Information | |
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Species | Capsella rubella |
Cazyme ID | Carubv10019759m |
Family | CBM45 |
Protein Properties | Length: 901 Molecular Weight: 101605 Isoelectric Point: 6.1478 |
Chromosome | Chromosome/Scaffold: 2 Start: 9738285 End: 9743071 |
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 | 318 | 394 | 2.4e-24 |
VHWGVCKNGGKRWEIPSEPYPEETSLFKNKALRTRLQQKDDGTGSFGVFSLDGKLEGLCFVLKLNENTWLNYRGEDF | |||
CBM45 | 133 | 214 | 1.5e-28 |
LHWGVSYVGDTGSEWDQPPEDMRPPGSIAIKDYAIETPLEKLSEGDFGVTISLNLESSVAALNFVLKDEETGAWYQHKGRDF | |||
GH13 | 532 | 819 | 3.5e-38 |
KASELAKLGFTVLWLPPPTESVSPEGYMPKDLYNLNSRYGTMDELKDTVRKFHKVGIKVLGDAVLNHRCAHFKNQNGVWNLFGGRLNWDDRAVVADDPHF QGRGNKSSGDNFHAAPNIDHSQDFVRKDIKEWLCWMREEVGYDGWRLDFVRGFWGGYVKDYMDASKPYFAVGEYWDSLSYTYGEMDYNQDAHRQRIVDWI NATSGAAGAFDVTTKGILHTALQKCEYWRLSDPKGKPPGVVGWWPSRAVTFVENHDTGSTQGHWRFPEGKEMQGYAYILTHPGTPAVF |
Full Sequence |
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Protein Sequence Length: 901 Download |
MSTVPIESLL HHSHLRNRHE SRTYRGTRSF LPCSLNLRSR FTSNKLLLLH SIGSGTSSGF 60 RSSKRRRSVA IRAGSSDTAV VETSQSDDVV FKENFSVRRI EKAEGKIYVR LKQVKENDWE 120 LSVGCSIPGK WILHWGVSYV GDTGSEWDQP PEDMRPPGSI AIKDYAIETP LEKLSEGDFG 180 VTISLNLESS VAALNFVLKD EETGAWYQHK GRDFKVPLVD DVPHNGNLIG AKKVFGSLGQ 240 LSNIPLEQEK SGAEVEEKSK SSSDSTKERK GLEEFYEEMP VSKHVADDNS VSVTARKCPE 300 TSKNIVSIET DLPGDVTVHW GVCKNGGKRW EIPSEPYPEE TSLFKNKALR TRLQQKDDGT 360 GSFGVFSLDG KLEGLCFVLK LNENTWLNYR GEDFYVPFLT SSSSPVETEA SQVSEHTRKT 420 DKEVSASGFT DEIITEIRNL AIDISHHKNQ KTNVKEVQEN ILQEIEKLAA EAYSIFRSTT 480 PTFTEESILE AEAEKPDIKI SSGTGSGFEI LCQGFNWESH KSGRWYLELQ EKASELAKLG 540 FTVLWLPPPT ESVSPEGYMP KDLYNLNSRY GTMDELKDTV RKFHKVGIKV LGDAVLNHRC 600 AHFKNQNGVW NLFGGRLNWD DRAVVADDPH FQGRGNKSSG DNFHAAPNID HSQDFVRKDI 660 KEWLCWMREE VGYDGWRLDF VRGFWGGYVK DYMDASKPYF AVGEYWDSLS YTYGEMDYNQ 720 DAHRQRIVDW INATSGAAGA FDVTTKGILH TALQKCEYWR LSDPKGKPPG VVGWWPSRAV 780 TFVENHDTGS TQGHWRFPEG KEMQGYAYIL THPGTPAVFF DHIFSDYHSE IASLLSLRNR 840 QKLHCRSEMN IDKSERDVYA AIIDDKVAMK IGPGHYEPPN GSQNWSVAVE GRDYKVWETS 900 * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PRK09441 | PRK09441 | 1.0e-47 | 509 | 840 | 413 | + cytoplasmic alpha-amylase; Reviewed | ||
PLN00196 | PLN00196 | 2.0e-136 | 500 | 898 | 416 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-162 | 510 | 847 | 341 | + 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 | 1.0e-172 | 506 | 898 | 399 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 900 | 907 | + 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 | AAG52558.1 | 3e-27 | 1 | 127 | 1 | 119 | AC010675_6 putative alpha-amylase; 60344-64829 [Arabidopsis thaliana] |
GenBank | AAG52558.1 | 0 | 163 | 900 | 95 | 826 | AC010675_6 putative alpha-amylase; 60344-64829 [Arabidopsis thaliana] |
RefSeq | NP_564977.1 | 0 | 1 | 900 | 1 | 887 | AMY3 (ALPHA-AMYLASE-LIKE 3); alpha-amylase [Arabidopsis thaliana] |
RefSeq | XP_002520134.1 | 0 | 1 | 900 | 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 | 509 | 898 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 509 | 898 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 509 | 898 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 509 | 898 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 509 | 898 | 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 | 849 | 69 | 901 | 0 |
HO826981 | 407 | 495 | 901 | 0 |
GR441435 | 293 | 453 | 745 | 0 |
ES805448 | 328 | 466 | 793 | 0 |
HO826981 | 27 | 464 | 490 | 0.14 |
Sequence Alignments (This image is cropped. Click for full image.) |
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