y
Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000148418 |
Family | GH13 |
Protein Properties | Length: 719 Molecular Weight: 82947.2 Isoelectric Point: 6.2354 |
Chromosome | Chromosome/Scaffold: 006837273 Start: 6187 End: 12116 |
Description | Alpha amylase family protein |
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 | 467 | 622 | 4.8e-23 |
FNDFTEKVLPHVKEAGYNTIQLMGVIEHKDYFTVGYRVTNLYAVSSRYGTPDDFKRLVDEAHGLGLLVFLDIVHSYSAADEMVGLSLFDGTNDCYFHAGK RGQHKYWGTRMFKYGDLDVLHFLLSNLNWWATEYQIDGFNFHSLSSMMYTHNGFAS |
Full Sequence |
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Protein Sequence Length: 719 Download |
MIVYEPAHLR MNSKFSNTSS SSFFVALLCP PPRQNSQYLL IPKPVSLRAA AALLSMTSLL 60 LSTKFSLYPN GTFLHFMFPN RPQRITFPRK TPIACSATEQ PKRRQKPPKK KKSVADGEKX 120 VDPVGFLTKH GISHKQFAQF LRERHKSVKD LTDEIFNRHA NLRDLASGFE ILGMHRHPEH 180 REDYMEWAPG ARYCALVGDF NGWSPTENCA REGHFGHDDY GYWFIILEDK LRDGEKPDEL 240 YFQQYNYIDD YDKGDSGVTI EELFKKANDE YWEPGEDXFI KNRFEMPAKL YEQIFGPNGP 300 QTLEELEEIP DAETRYKSWK EQHKDDIPSN APCYDVIDNG KEYDIFNVVL DPVSQEKFRG 360 KKPPLAYWFE TRKGRKAWLK KYSPCIPHGS KYRVYFNTPS GPLERVPAWA TYVQPEAEGE 420 QAFAIHWEPP PEYAFKWKNS RPKVPKSLRI YECHVGISGS EPKMTSFNDF TEKVLPHVKE 480 AGYNTIQLMG VIEHKDYFTV GYRVTNLYAV SSRYGTPDDF KRLVDEAHGL GLLVFLDIVH 540 SYSAADEMVG LSLFDGTNDC YFHAGKRGQH KYWGTRMFKY GDLDVLHFLL SNLNWWATEY 600 QIDGFNFHSL SSMMYTHNGF ASFTGDLEEY CNQYVDKDAL LYLILANEIL HVLHPNIITI 660 AEDATFYPGL CEPISQGGLG FDYCVNLSVS ETWSNFLENV PDHDWSMSKV EPFNCDTLS 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 6.0e-13 | 135 | 237 | 103 | + 1,4-alpha-glucan-branching enzyme | ||
PLN02447 | PLN02447 | 1.0e-129 | 383 | 710 | 332 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 1.0e-130 | 431 | 710 | 281 | + Alpha amylase catalytic domain found in bacterial and eukaryotic branching enzymes. Branching enzymes (BEs) catalyze the formation of alpha-1,6 branch points in either glycogen or starch by cleavage of the alpha-1,4 glucosidic linkage yielding a non-reducing end oligosaccharide chain, and subsequent attachment to the alpha-1,6 position. By increasing the number of non-reducing ends, glycogen is more reactive to synthesis and digestion as well as being more soluble. This group includes bacterial and eukaryotic proteins. 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. | ||
PLN02960 | PLN02960 | 0 | 63 | 710 | 651 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 63 | 710 | 656 | + alpha-amylase; Provisional |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
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 |
DDBJ | BAB02827.1 | 0 | 56 | 709 | 1 | 659 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 56 | 710 | 1 | 657 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 56 | 710 | 1 | 660 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002278858.1 | 0 | 56 | 710 | 1 | 627 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002529457.1 | 0 | 56 | 710 | 1 | 661 | 1,4-alpha-glucan branching enzyme, 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 | 3amk_A | 0 | 384 | 710 | 114 | 447 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 384 | 710 | 114 | 447 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 384 | 710 | 114 | 447 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY965821 | 293 | 314 | 606 | 0 |
BF272517 | 278 | 405 | 682 | 0 |
JG636329 | 270 | 392 | 661 | 0 |
CO104525 | 273 | 432 | 704 | 0 |
EH718768 | 263 | 410 | 672 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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