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Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma04g01950.2 |
Family | GH13 |
Protein Properties | Length: 899 Molecular Weight: 101593 Isoelectric Point: 4.7575 |
Chromosome | Chromosome/Scaffold: 04 Start: 1335714 End: 1344458 |
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 | 286 | 611 | 4.8e-29 |
LPRIRANNYNTVQLMAVMEHSYYASFGYHVTNFFAVSSRSGTPEDLKYLIDKAHSLGLQVLMDVIHSHASNNVTDGLNGFDVGQTSQDSYFHTGDRGYHK LWDSRLFNYANWEVLRFLLSNLRWWLEEFKFDGFRFDGVTSMLYHHHGINIAFTGDYNEYFSEATDVDAVVYLMLANCLIHSILPDATVIAEDVSGMPGL GQPVSDGGIGFDYRLAMAIPDKWIDYLKNKNDYAWSMKEISWSLTNRRYTEKCVSYAESHDQAIVGDKTVAFLLMDEEMYSGMSSLVDASPIVERGIALQ KMIHFITMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 899 Download |
MINCLGLYPL ISAPSTIACT THIVRSKQYL ATQKPVNLAL GYRNPHGYGF SFGSRRSIHE 60 RVSSHFKGIA VMTDDKSTMS STEEDLENIG IFHIDPSLKP YKDHFKYRLK RYVDQKKLIE 120 EYEGGLEEFS QGYLKFGFNR EEGGIVYCEW APAAQEAQII GDFNGWDGSN HQMEKNQFGV 180 WSIRIPDTDG NSAIPHNSRV KFRFRHGDGV WVDRIPAWIK YATVDPTRFA APYDGVYWDP 240 PLSERYQFKY PRPPKPKAPR IYEAHVGMSS FEPRINSYRE FADEILPRIR ANNYNTVQLM 300 AVMEHSYYAS FGYHVTNFFA VSSRSGTPED LKYLIDKAHS LGLQVLMDVI HSHASNNVTD 360 GLNGFDVGQT SQDSYFHTGD RGYHKLWDSR LFNYANWEVL RFLLSNLRWW LEEFKFDGFR 420 FDGVTSMLYH HHGINIAFTG DYNEYFSEAT DVDAVVYLML ANCLIHSILP DATVIAEDVS 480 GMPGLGQPVS DGGIGFDYRL AMAIPDKWID YLKNKNDYAW SMKEISWSLT NRRYTEKCVS 540 YAESHDQAIV GDKTVAFLLM DEEMYSGMSS LVDASPIVER GIALQKMIHF ITMALGGEGY 600 LNFMGNEFGH PEWIDFPREG NGWSYEKCRR QWNLVDTDHL RYKFMNAFDR AMNLLDDKFS 660 FLASTKQIVS SADDDDKVIV FERGDLIFVF NFHPENTYEG YKVGCDLPGK YRVALDSDAW 720 EFGGRGRVGH DVDHFTSPEG IPGVPETNFN NRPNSFKVLS PARTCVAYYR VEESQEDDDN 780 NSLVGVEETS AAADVAKIPD ESASTESEDI KLDGVKETLA AADVAKIPDE SAPLESEDSN 840 LDVVKEPLAA ANAEVTKISG ELVSVETEGI NLDKLEETIV AASVESEVVR DKPEDAAN* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 2.0e-7 | 108 | 187 | 86 | + alpha-amylase | ||
PLN03244 | PLN03244 | 6.0e-133 | 193 | 731 | 543 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 69 | 779 | 711 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 243 | 650 | 408 | + 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 | 193 | 769 | 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 | AAT76445.1 | 0 | 1 | 728 | 1 | 728 | starch branching enzyme I [Vigna radiata] |
DDBJ | BAA82349.1 | 0 | 1 | 855 | 1 | 847 | starch branching enzyme [Phaseolus vulgaris] |
EMBL | CAA54308.1 | 0 | 1 | 832 | 1 | 834 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CAA56320.1 | 0 | 22 | 863 | 8 | 823 | starch branching enzyme II [Pisum sativum] |
EMBL | CBI18866.1 | 0 | 1 | 811 | 1 | 821 | unnamed protein product [Vitis vinifera] |
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 | 79 | 823 | 1 | 751 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 79 | 777 | 1 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 79 | 777 | 1 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 79 | 777 | 1 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 1.96182e-44 | 144 | 724 | 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 | 693 | 175 | 863 | 0 |
HO794536 | 721 | 91 | 799 | 0 |
HO777638 | 669 | 143 | 799 | 0 |
CX109187 | 442 | 388 | 823 | 0 |
HO777638 | 47 | 94 | 140 | 0.021 |
Sequence Alignments (This image is cropped. Click for full image.) |
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