Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.005G251000.1 |
Family | GH13 |
Protein Properties | Length: 862 Molecular Weight: 97229.1 Isoelectric Point: 5.1977 |
Chromosome | Chromosome/Scaffold: 05 Start: 25329841 End: 25336292 |
Description | starch branching enzyme 2.2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 291 | 616 | 4.7e-29 |
LPRIRANNYNTVQLMAVIEHSYYASFGYHVTNFFAVSSRSGNPEDLKYLIDKAHSLGLRVLMDVVHSHASNNVTDGLNGFDIGQGAQESYFHTGDRGYHN LWDSRLFNYANWEVLRFLLSNLRWWLEEFKFDGFRFDGVTSMLYHHHGINMAFTGDYNEYFSEATDVDAVVYLMLANYLIHNILPDATVIAEDVSGMPGL GCPVSEGGVGFDYRLAMAIPDKWIDYLKNKSDLEWSMNEISRSLTNRRYTEKCVAYAESHDQSIVGDKTIAFILMDKEMYSGMSCLTEAPPAVDRGIALH KMIHFITMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 862 Download |
MLGSSSGLLP APPLLPSVAE NSKWVCAIRY KRCTAKEKPV RLPSGGSKKL LCHSRFCFPL 60 RISNNDRVRH GFAISAVLTD DPTMTTVGDG LENIGLVSID PGLESFKDHF RYRMKRYVDQ 120 KNLIERYEGG LEEFALGYQK FGFNRDEGGI VYREWAPAAQ EAQIIGDFNG WDGSNHRMEK 180 NEFGVWSIKI PDSGGNPAIP HDSRVKFRFM QGNGVWVDRI PAWIKCATVD PASFGAPYDG 240 VYWDPPTSER YEFKFPRPPK PNAPRIYEAH VGMSSSEPRV NSYREFADNV LPRIRANNYN 300 TVQLMAVIEH SYYASFGYHV TNFFAVSSRS GNPEDLKYLI DKAHSLGLRV LMDVVHSHAS 360 NNVTDGLNGF DIGQGAQESY FHTGDRGYHN LWDSRLFNYA NWEVLRFLLS NLRWWLEEFK 420 FDGFRFDGVT SMLYHHHGIN MAFTGDYNEY FSEATDVDAV VYLMLANYLI HNILPDATVI 480 AEDVSGMPGL GCPVSEGGVG FDYRLAMAIP DKWIDYLKNK SDLEWSMNEI SRSLTNRRYT 540 EKCVAYAESH DQSIVGDKTI AFILMDKEMY SGMSCLTEAP PAVDRGIALH KMIHFITMAL 600 GGEGYLNFMG NEFGHPEWID FPREGNGWSY EMCRRQWNLA DMEHLRYKFM NAFDRAMNLL 660 DEKYSFLAST KQIVSSTNEE DKVIVFERGD LVFVFNFHPE KTYDGYKVGC DLPGKYRVAL 720 DSDALEFGGH GRVGHDADHF TSPEGIPGVP ETNFNNRPNS FKVLSPARTC VVYYRVEESE 780 ESHDDDDEMG LNEILAADVI PEQEDVEEAA SQAKVGKPHL VDGDGDGDGD GDGDGSGLKL 840 KILGMMHRMI KNLHPTSDYT S* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 7.0e-9 | 106 | 192 | 93 | + alpha-amylase | ||
PLN03244 | PLN03244 | 2.0e-140 | 197 | 773 | 582 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 38 | 776 | 739 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 247 | 655 | 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. | ||
PLN02960 | PLN02960 | 0 | 197 | 774 | 583 | + alpha-amylase |
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 |
GenBank | ABN05321.1 | 0 | 1 | 821 | 1 | 819 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 1 | 824 | 1 | 832 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 5 | 823 | 4 | 827 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 31 | 823 | 9 | 804 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002307789.1 | 0 | 84 | 786 | 1 | 701 | predicted protein [Populus trichocarpa] |
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 | 3aml_A | 0 | 84 | 816 | 1 | 728 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 84 | 781 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 84 | 781 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 84 | 781 | 1 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 0 | 149 | 729 | 26 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch biosynthesis | RXN-7710 | EC-2.4.1.18 | 1,4-α-glucan branching enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO619167 | 641 | 180 | 814 | 0 |
HO794536 | 690 | 96 | 773 | 0 |
HO777638 | 638 | 148 | 773 | 0 |
CX109187 | 384 | 393 | 776 | 0 |
HO777638 | 47 | 99 | 145 | 0.083 |
Sequence Alignments (This image is cropped. Click for full image.) |
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