y
Basic Information | |
---|---|
Species | Prunus persica |
Cazyme ID | ppa001929m |
Family | GH13 |
Protein Properties | Length: 741 Molecular Weight: 84614.5 Isoelectric Point: 4.9455 |
Chromosome | Chromosome/Scaffold: 1 Start: 31926433 End: 31931512 |
Description | starch branching enzyme 2.2 |
View CDS |
External Links |
---|
NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH13 | 206 | 531 | 6.6e-29 |
LPRIRANNYNTVQLMAVMEHSYYASFGYHVTNFFAVSSRSGTPEDLKYLIDKAHCLGLRVLMDVVHSHASNNVTDGLNGFEVGQSSQESYFHTGDRGYHK LWDSRLFNYSNWEVLRFLLSNLRWWLEEFKFDGFRFDGVTSMLYHHHGINMAFTGDYHEYFSEATDVDAVVYLMLANYLIHKILPDATVIAEDVSGMPGL GRPVSEGGIGFDYRLAMAIPDKWIDYLKNKNDEEWSMNEISCSLTNRRYTEKCISYAESHDQAIVGDKTIAFFLMDREMYSGMSCLTDASPTIERGIALH KMIHFLTMALGGEGYLNFMGNEFGHP |
Full Sequence |
---|
Protein Sequence Length: 741 Download |
MTDEEMESIG ILSIDQALEP YKEHFKYRIK KYVDQKGLIE TYEGGLEEFA QGYVKFGFNR 60 EEDGIVYREW APAAQEAQLI GDFNGWDGSK HKMEKNQYGV WSIKIPNSGG NSAIPHNSRV 120 KFRFKHGNEV WVDRIPAWIK YATVDPARFA APYDGVYWDP PPSERFQFKH PHPPKPKAPR 180 IYEAHVGMSS SEPQISSYRE FADDVLPRIR ANNYNTVQLM AVMEHSYYAS FGYHVTNFFA 240 VSSRSGTPED LKYLIDKAHC LGLRVLMDVV HSHASNNVTD GLNGFEVGQS SQESYFHTGD 300 RGYHKLWDSR LFNYSNWEVL RFLLSNLRWW LEEFKFDGFR FDGVTSMLYH HHGINMAFTG 360 DYHEYFSEAT DVDAVVYLML ANYLIHKILP DATVIAEDVS GMPGLGRPVS EGGIGFDYRL 420 AMAIPDKWID YLKNKNDEEW SMNEISCSLT NRRYTEKCIS YAESHDQAIV GDKTIAFFLM 480 DREMYSGMSC LTDASPTIER GIALHKMIHF LTMALGGEGY LNFMGNEFGH PEWVDFPREG 540 NGWSYEKCRR QWNLVDTDHL RYKFMNAFDR AMNLLDEKFS FLSSTQQIVS STNEEDKVIV 600 FERGDLVFVF NFHPENTYDG YKVGCDLPGK YRVALDSDAY EFGGHGRVGH DVDHFTFPEG 660 IPGVPETNFN NRPNSFKVLS PAHTCVVYYR VDESLEADVD ETSIAEVVVG KENFEELGSV 720 IDDGNVGPRA EKSGEGSSDD * 780 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 1.0e-6 | 28 | 105 | 84 | + alpha-amylase | ||
PLN03244 | PLN03244 | 3.0e-130 | 113 | 642 | 534 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 7.0e-180 | 113 | 638 | 533 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 4 | 700 | 697 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 162 | 570 | 409 | + 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. |
Gene Ontology | |
---|---|
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 | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | AAZ20130.1 | 0 | 2 | 740 | 98 | 838 | starch branching enzyme I [Malus x domestica] |
GenBank | ABN05321.1 | 0 | 6 | 719 | 89 | 809 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 3 | 693 | 87 | 777 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 4 | 722 | 91 | 817 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 4 | 722 | 68 | 794 | PREDICTED: hypothetical protein [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3aml_A | 0 | 4 | 696 | 6 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 4 | 696 | 6 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 4 | 696 | 6 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 4 | 696 | 6 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 9.94922e-44 | 64 | 644 | 26 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
EST Download unfiltered results here | ||||
---|---|---|---|---|
Hit | Length | Start | End | EValue |
HO619167 | 625 | 95 | 717 | 0 |
HO794536 | 707 | 11 | 705 | 0 |
HO777638 | 654 | 64 | 705 | 0 |
CX109187 | 389 | 308 | 696 | 0 |
HO777638 | 47 | 14 | 60 | 2.1 |
Sequence Alignments (This image is cropped. Click for full image.) |
---|