Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000162817 |
Family | GH13 |
Protein Properties | Length: 1561 Molecular Weight: 174419 Isoelectric Point: 6.5659 |
Chromosome | Chromosome/Scaffold: 000416247 Start: 9652 End: 19768 |
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 | 633 | 919 | 2.5e-36 |
ALLSSLGFTVIWFPPPTESVSPEGYMPRDLYNLNSRYGNMDELKETVKVFHDVGIKVLGDAVLNHRCAHYRNQNGVWNIFGGRLNWDDRAVVADDPHFQG RGNKSSGDSFHAAPNIDHSQDFVRKDIREWLCWLRNDIGYDGWRLDFVRGFWGGYVRDYVDASEPYFAVGEYWDSLSYTYGEMDRNQDAHRQRIVDWINA TNGTCGAFDVTTKGILHAALERCEYWRLSDEKGKPPGVLGWWPSRAVTFIENHDTGSTQGHWRFPKGKEMQGYAYILTHPGTPTVFY | |||
PL1 | 1275 | 1480 | 0 |
IQKGPLWIIFTKSMVIRLQQELMVTSDKTIDARGANVVIEEGAGITLQFVKNVIITNLHIKMIVTKPGGLIRDSVDHIGLRTQSDGDGISLFGASNVWID HVSMSRCADGLIDAIMGSTAITISNSHFTDHDEAMLFGANNAHTQDKIMQITLAFNHFGQGLVQRMPRVRHGFFHVVNNDYTHWIMYAIGGNMNPTIISQ GNRFIA |
Full Sequence |
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Protein Sequence Length: 1561 Download |
MSTVRIEPLL QDLHHYGRQK PSHRRPQSNH PLKLSSSFTA FPKKLVVSNS RSFCYFQPPT 60 PRRGPTLGVR AASTDTTTVE TSESTDPIYK KTFPLKRTEV VEGKIFVKLD HGKNEKKWVL 120 TVGCNLPGKW VLHWGVSFVD DVSCEWEQPP SEMRPAGSVP IKVCNWVLKF DCRAVGWNEF 180 DIHEDFQDYA IETPLKESLS SVGGDTSYEV KIDVKPNSAI AAINFVLKVV IFNYVCSCWG 240 VLVLQDEETG AWYQHRGSDF RVPLVAYPQD DDNVVGATKG FGMWPVKPSV CLAVVAKILE 300 PTNTHSFLAV EEMGYGVLGK LSNVFVKAES SNSKDQDSSG SESRHPQQKT TCVEGFYEEL 360 PIAKEISVNN SVTVSVSKCP ETAKNLLYLE TDLPDNAVVH WGVCRDDTKT WEIPAAPHPP 420 ETVVFKDKAL RTRLQHKGLF IQSGMLSEQQ KEGGNGCWGL FTLEEGLAGF LFLLKLNEST 480 WLRCVGNDFY IPLSSSKNAN VVQSEIQSKD AQVPDGSTEA VEESTAYADG LINEMRNLVS 540 DVFSDKSPRT RSKKAQEAIL QEIEKLAAEA YSIFRTTVPT LPEETIAETE EVKVAPAKIC 600 SGTGTGFEIL CQGFNWESSK SGRWYMELKS KAALLSSLGF TVIWFPPPTE SVSPEGYMPR 660 DLYNLNSRYG NMDELKETVK VFHDVGIKVL GDAVLNHRCA HYRNQNGVWN IFGGRLNWDD 720 RAVVADDPHF QGRGNKSSGD SFHAAPNIDH SQDFVRKDIR EWLCWLRNDI GYDGWRLDFV 780 RGFWGGYVRD YVDASEPYFA VGEYWDSLSY TYGEMDRNQD AHRQRIVDWI NATNGTCGAF 840 DVTTKGILHA ALERCEYWRL SDEKGKPPGV LGWWPSRAVT FIENHDTGST QGHWRFPKGK 900 EMQGYAYILT HPGTPTVFYD HIFSHYQSEI AALISLRNRN KLNCRSLVKI TKAERDVYAA 960 IIDEKVAIKI GPGHYEPASG PQNWNKSLEG GDYKVWEASL VFSAPTRSTE DGAGGADRXA 1020 SAVQNRGQSA ECGSGEHGFW RVSTHIKRHP PDKPIDKLVG KLIISCDGFN LLAWLGWVCF 1080 DTLEQPCPRP TQQFPCRKVS GAADEVPTTM VAMFNSSYFF LFLFFLYFAV FVSSNDNPTD 1140 VPNEDTLVLD LDAYWKERAE EAEKVAMESY NKNPEKVTEE FNTEVGKLMS KENTTRRNLR 1200 GNKAYTGPCM ATNPMDACWR CDPNWANNRK KIVGCAQGFG KKTTGGKDGP FYVVTMGTDD 1260 DVQNPKPGTL RHAVIQKGPL WIIFTKSMVI RLQQELMVTS DKTIDARGAN VVIEEGAGIT 1320 LQFVKNVIIT NLHIKMIVTK PGGLIRDSVD HIGLRTQSDG DGISLFGASN VWIDHVSMSR 1380 CADGLIDAIM GSTAITISNS HFTDHDEAML FGANNAHTQD KIMQITLAFN HFGQGLVQRM 1440 PRVRHGFFHV VNNDYTHWIM YAIGGNMNPT IISQGNRFIA PINGVTKQVT HRENTPEAEW 1500 KNWEWRSEGD LMMNGAFFVE SGSGASKHPA KLDXMPFKPG TXVXTLTKFS GALNCAVGKP 1560 C |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00656 | Amb_all | 2.0e-75 | 1288 | 1482 | 206 | + Amb_all domain. | ||
PLN00196 | PLN00196 | 1.0e-127 | 608 | 997 | 403 | + alpha-amylase; Provisional | ||
cd11314 | AmyAc_arch_bac_plant_AmyA | 6.0e-152 | 609 | 948 | 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 | 3.0e-152 | 606 | 997 | 398 | + alpha-amylase | ||
PLN02784 | PLN02784 | 0 | 1 | 999 | 999 | + 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:0030570 | pectate lyase activity |
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 | 1 | 999 | 1 | 901 | plastid alpha-amylase [Malus x domestica] |
GenBank | AAX33233.1 | 0 | 1 | 999 | 1 | 895 | plastid alpha-amylase [Actinidia chinensis] |
EMBL | CBI32016.1 | 0 | 1 | 999 | 1 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002270049.1 | 0 | 1 | 999 | 1 | 901 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002520134.1 | 0 | 1 | 999 | 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 | 608 | 997 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_B | 0 | 608 | 997 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 2qpu_A | 0 | 608 | 997 | 2 | 403 | A Chain A, Sugar Tongs Mutant S378p In Complex With Acarbose |
PDB | 3bsg_A | 0 | 608 | 1008 | 2 | 414 | A Chain A, Barley Alpha-Amylase Isozyme 1 (Amy1) H395a Mutant |
PDB | 1rpk_A | 0 | 608 | 997 | 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 | 1005 | 1 | 1005 | 0 |
HO826981 | 402 | 598 | 999 | 0 |
HO811991 | 298 | 702 | 999 | 0 |
HO826981 | 30 | 562 | 591 | 1 |
EG631183 | 18 | 1021 | 1038 | 4.6 |
Sequence Alignments (This image is cropped. Click for full image.) |
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