Basic Information | |
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Species | Prunus persica |
Cazyme ID | ppa016544m |
Family | GH13 |
Protein Properties | Length: 878 Molecular Weight: 101093 Isoelectric Point: 6.2691 |
Chromosome | Chromosome/Scaffold: 4 Start: 13759016 End: 13767484 |
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 | 405 | 737 | 8.6e-23 |
SEPKISSFSDFIEKVLPHVKEAGYNTIQLIGVIEHKDYFTVGYRATNLYAVSSRYGTPDDFKRLVDEAHGLGLLVFLDIVHSYSAADEMVGLSLFDGTND CYFHTGKRGHHKYWGTRMFKYGDLDVLHFLLSNLNWWPTEYQIDGFHFHSLSSMMYTHNGFASFTGDLEEYCNQYVDKDALLYLILANEILHALHPDIIT IAEDATFYPGLCEPTSQGGLGFDYCVNLSVSEMWSSFLETVPDHDWSMTKIVNTLMGNRKFADKTLVYAENHNQSISGGRSFAEILFGEIRDGSHDTEKL LLRGCSLHKMIRLITLTIGGRAYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 878 Download |
MTSLSLSTKF SLYPNSTFLQ FQFPNRTQRI SFPKKTQIAC SATEQPKGQQ KRPKKKKSVT 60 DSEKGIDPVG FLTKFGISHK QFSQFLRERH KSLKDLTDEI FNRHIDLRDM ASGFEILGIH 120 RHPEHREDYM EWAPGARYCA LVGDFNGWSP TENCAREGHF GHDDYGYWFI ILEDKLRDGE 180 KPDELYFQQY NYIDDYDKGD SGVPIEEIFK KANDEYWEPG EDRFIKNRYE IPAKLYEQIF 240 GPNGPQTLEE LEEIPDAETR YKAWKEQHKD DLPSNTPCYD VIDNGKEYDI FNVVLDPVSQ 300 EKFRAKKPPL AYWLETRKGR QAWLKKYSPC IPHGSKYRVY FNTPSGPLER VPAWATYVQP 360 DAEGEQAFAI HWDPPPEYAY KWKNSRPKVP KSLRIYECHV GISGSEPKIS SFSDFIEKVL 420 PHVKEAGYNT IQLIGVIEHK DYFTVGYRAT NLYAVSSRYG TPDDFKRLVD EAHGLGLLVF 480 LDIVHSYSAA DEMVGLSLFD GTNDCYFHTG KRGHHKYWGT RMFKYGDLDV LHFLLSNLNW 540 WPTEYQIDGF HFHSLSSMMY THNGFASFTG DLEEYCNQYV DKDALLYLIL ANEILHALHP 600 DIITIAEDAT FYPGLCEPTS QGGLGFDYCV NLSVSEMWSS FLETVPDHDW SMTKIVNTLM 660 GNRKFADKTL VYAENHNQSI SGGRSFAEIL FGEIRDGSHD TEKLLLRGCS LHKMIRLITL 720 TIGGRAYLNF MGNEFGHPEV RGLSSQCQAT ISRFHLPSDL MNLDENERVL TRVLLSIHHV 780 NDDNMVIAYL RGPLLFVFNF HPTDSYEGYR IGVEEAGEYQ LVLNTDEIKY GGQGLIKDDQ 840 YLRKTISKRG DGLRNCLEVP MPSRTAQVYK LSRILRI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 2.0e-12 | 80 | 182 | 103 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 1.0e-162 | 376 | 739 | 369 | + 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 | 1 | 877 | 897 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 1 | 877 | 902 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 328 | 869 | 572 | + 1,4-alpha-glucan-branching enzyme |
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 | 1 | 877 | 1 | 903 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 1 | 877 | 1 | 896 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 1 | 877 | 1 | 899 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002278858.1 | 0 | 1 | 877 | 1 | 866 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002529457.1 | 0 | 1 | 868 | 1 | 892 | 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 | 329 | 839 | 114 | 653 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 329 | 839 | 114 | 653 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 329 | 839 | 114 | 653 | 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 |
BF272517 | 278 | 350 | 627 | 0 |
DY965821 | 293 | 259 | 551 | 0 |
JG636329 | 270 | 337 | 606 | 0 |
CO104525 | 273 | 377 | 649 | 0 |
EH718768 | 263 | 355 | 617 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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