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Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10016249m |
Family | GH13 |
Protein Properties | Length: 836 Molecular Weight: 94835 Isoelectric Point: 5.4284 |
Chromosome | Chromosome/Scaffold: 10 Start: 8656467 End: 8662881 |
Description | starch branching enzyme 2.1 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 333 | 654 | 3.5e-29 |
LPRIKKLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPDDLKSLIDKAHELGLVVLMDIVHSHASKNTLDGLNMFDGTDGQYFHSGTRGYHWMWD SRLFNYGSWEVLRYLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVEFTGNYNEYFGYSTDVDAVVYLMLVNDMIHGLYPEAIVVGEDVSGMPAFCIP VQDGGVGFDYRLHMAVADKWIELLKKRDEDWQVGDIVFTLTNRRWGEKCVVYAESHDQALVGDKTIAFWLMDKDMYDFMAVDRQATPRVDRGIALHKMIR LITMGLGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 836 Download |
MVYTISGVRL PRLPSIKSSS LPSFSEDRRS NAVSFPLRKE SRSSGKVFAR KPSHDSESSS 60 LATSASEKLG GHQSDNSSAV TDQVELRETV SEDTQVQDQT SALSTSGGQN YKANIASMSE 120 SFVQEGGQRR IPPPGDGKKI YDIDPMLNSH HGHLDYRYGQ YKKLREEIDK NEGGLEAFSR 180 GYEIFGFTRS TTGITYREWA PGAKAASLIG DFNNWNSKAD VMTRNEFGVW EIFLPNDADG 240 SPAIPHGSRV KIRMDTPSGI KDSIPAWIKY SVQAPGEIPY NGVYYDPAEE DKHVFKHPRP 300 KRPKSLRIYE SHVGMSSTEP MINTYANFRD DVLPRIKKLG YNAVQIMAIQ EHSYYASFGY 360 HVTNFFAPSS RFGTPDDLKS LIDKAHELGL VVLMDIVHSH ASKNTLDGLN MFDGTDGQYF 420 HSGTRGYHWM WDSRLFNYGS WEVLRYLLSN ARWWLEEYKF DGFRFDGVTS MMYTHHGLQV 480 EFTGNYNEYF GYSTDVDAVV YLMLVNDMIH GLYPEAIVVG EDVSGMPAFC IPVQDGGVGF 540 DYRLHMAVAD KWIELLKKRD EDWQVGDIVF TLTNRRWGEK CVVYAESHDQ ALVGDKTIAF 600 WLMDKDMYDF MAVDRQATPR VDRGIALHKM IRLITMGLGG EGYLNFMGNE FGHPEWIDFP 660 RTDQHLPDGR VIPGNNGSYD KCRRRFDLGD AEYLRYHGLQ EFDRAMQHLE ENYGFMTSEH 720 QYISCKDEGD RVIVFERGNL VFVFNFHWTN SYSDYRIGCS VPGKYKIVLD SDDSLFGGFN 780 RLDDSAEFFT SDGRYDDRPC SFMVYAPCRT AVVYAAVEGD EDSSLVPISL VPEDV* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 2.0e-9 | 157 | 234 | 84 | + alpha-amylase | ||
PLN03244 | PLN03244 | 1.0e-138 | 242 | 814 | 581 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 71 | 835 | 770 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 289 | 704 | 417 | + 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 | 242 | 814 | 577 | + 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 | AAB03099.1 | 0 | 8 | 835 | 4 | 854 | starch branching enzyme class II [Arabidopsis thaliana] |
GenBank | ABO31358.1 | 0 | 1 | 819 | 1 | 841 | starch branching enzyme II-1 [Malus x domestica] |
GenBank | ABO31359.1 | 0 | 1 | 825 | 1 | 847 | starch branching enzyme II-2 [Malus x domestica] |
EMBL | CAA56319.1 | 0 | 1 | 830 | 1 | 855 | starch branching enzyme I [Pisum sativum] |
RefSeq | NP_181180.1 | 0 | 1 | 835 | 1 | 858 | SBE2.1 (starch branching enzyme 2.1); 1,4-alpha-glucan branching enzyme [Arabidopsis thaliana] |
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 | 136 | 822 | 9 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 136 | 822 | 9 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 136 | 822 | 9 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 140 | 822 | 13 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 1m7x_D | 0 | 180 | 780 | 9 | 579 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 692 | 134 | 825 | 0 |
HO777638 | 636 | 190 | 825 | 0 |
HO458123 | 395 | 423 | 817 | 0 |
HO458123 | 296 | 134 | 422 | 0 |
HO777638 | 47 | 143 | 189 | 0.0000000006 |
Sequence Alignments (This image is cropped. Click for full image.) |
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