y
Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM5G863596_T02 |
Family | CBM45 |
Protein Properties | Length: 742 Molecular Weight: 84006.1 Isoelectric Point: 5.3622 |
Chromosome | Chromosome/Scaffold: 3 Start: 202942770 End: 202965565 |
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 | 163 | 241 | 8.4e-22 |
IHWGVCRDNTMTWEIPPEPHPPKTKIFRHKALQTLLQQKADGAGNSISFSLDAEYSCLFFVLKLDEYTWLRNLENGSDF | |||
GH13 | 376 | 661 | 2.8e-37 |
ELSSLGFTIVWSPPPTDSVSPEGYMPRDLYNLNSRYGSMDELKELVKIFHEAGIKVLGDAVLNHRCAQFQNNNGVWNIFGGRMNWDDRAVVADDPHFQGR GNKSSGDNFHAAPNIDHSQEFVRNDLKEWLCWMRKEVGYDGWRLDFVRGFWGGYVKDYLEASEPYFAVGEYWDSLSYTYGEMDYNQDAHRQRIVDWINAT NGTAGAFDVTTKGILHAALERSEYWRLSDEKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPYGMELQGYAYILTHPGTPAVFY |
Full Sequence |
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Protein Sequence Length: 742 Download |
MRPPGSVAIK DYAIETPLEI LPNSEGQPLY EMQIKFDKDI PIAAVNFVLK EEETGAWFQH 60 KGRDFRIPLN GSFNDGGKQD IDIWPGDLGH VLKKSEGSSS QPQNTSPEDT GLSGKHISGF 120 YEEYPILKSE YVQNLVTVTV RRDIEAHKRL VEFDTDIPGE VIIHWGVCRD NTMTWEIPPE 180 PHPPKTKIFR HKALQTLLQQ KADGAGNSIS FSLDAEYSCL FFVLKLDEYT WLRNLENGSD 240 FYVPLTRVGQ YGSTQDPDKA EAQKIEDKSS QADGLISDIR NLVVGLSSRR GQKAKNKVLQ 300 EDILQEIERL AAEAYSIFRS PTIDSVDESV QLDDTLSAKP ACSGTGSGFE ILCQGFNWES 360 HKSGKWYVEL GTKAKELSSL GFTIVWSPPP TDSVSPEGYM PRDLYNLNSR YGSMDELKEL 420 VKIFHEAGIK VLGDAVLNHR CAQFQNNNGV WNIFGGRMNW DDRAVVADDP HFQGRGNKSS 480 GDNFHAAPNI DHSQEFVRND LKEWLCWMRK EVGYDGWRLD FVRGFWGGYV KDYLEASEPY 540 FAVGEYWDSL SYTYGEMDYN QDAHRQRIVD WINATNGTAG AFDVTTKGIL HAALERSEYW 600 RLSDEKGKPP GVLGWWPSRA VTFIENHDTG STQGHWRFPY GMELQGYAYI LTHPGTPAVF 660 YDHIFSHLQP EIAKFISIRH RQKIHCRSKI KILKAERSLY AAEIDEKVTM KIGSEHFEPS 720 GPQNWIVAAE GQDYKIWEAS S* 780 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02784 | PLN02784 | 6.0e-9 | 65 | 245 | 190 | + alpha-amylase | ||
PLN00196 | PLN00196 | 1.0e-136 | 350 | 738 | 406 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 2.0e-160 | 351 | 690 | 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 | 8.0e-172 | 347 | 738 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 740 | 759 | + 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 | EEC71386.1 | 0 | 1 | 741 | 138 | 876 | hypothetical protein OsI_03507 [Oryza sativa Indica Group] |
GenBank | EEC71386.1 | 0.008 | 88 | 252 | 49 | 211 | hypothetical protein OsI_03507 [Oryza sativa Indica Group] |
RefSeq | NP_001044062.1 | 0 | 1 | 741 | 138 | 876 | Os01g0715400 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002456247.1 | 0 | 1 | 741 | 79 | 820 | hypothetical protein SORBIDRAFT_03g032830 [Sorghum bicolor] |
RefSeq | XP_002456247.1 | 0.007 | 136 | 258 | 32 | 160 | 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 | 350 | 738 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 350 | 738 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1p6w_A | 0 | 350 | 738 | 2 | 403 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1ht6_A | 0 | 350 | 738 | 2 | 403 | A Chain A, Crystal Structure At 1.5a Resolution Of The Barley Alpha- Amylase Isozyme 1 |
PDB | 2qps_A | 0 | 350 | 738 | 2 | 403 | A Chain A, "sugar Tongs" Mutant Y380a In Complex With Acarb |