Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma19g37750.2 |
Family | GH13 |
Protein Properties | Length: 869 Molecular Weight: 98813 Isoelectric Point: 5.3623 |
Chromosome | Chromosome/Scaffold: 19 Start: 44843020 End: 44861927 |
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 | 360 | 680 | 7.3e-30 |
LPRIKRLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPEELKSLIDRAHELGLLVLMDIVHSHASNNTLDGLNMFDGTDGHYFHPGSRGYHWMWD SRLFNYGSWEVLRYLLSNARWWLDEYKFDGFRFDGVTSMMYTHHGLEVAFTGNYNEYFGFATDVDAVVYLMLTNDVIHGLFPEAVTIGEDVSGMPTFCLP TQDGGIGFDYRLHMAIADKWIEILKKNDEDWKMGDIIHTLTNRRWLEKCVAYAESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPIIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 869 Download |
MVYTISGIRF PVLPSLHNSR FRGDRRTASL PVFLRNNSFS RKTLALKSSH DSDSLSSAIA 60 KSDKVLIPQD QDNSASLTDQ LETPDITSED TQNLEDLTME DEDKYNISEA ASSYRHIEDG 120 QGSVVSSLVD VNIPAKKASV SVGRKSKIVS DEVKPKIIPP PGTGQKIYEI DPSLLAHRDH 180 LDFRYGQYKR LCYEIDKHEG GLDTFSRGYE KFGFIRSATG ITYREWAPGA KSAALIGDFN 240 NWNPNADVMT RNEFGVWEIF LPNNVDGSPP IPHGSRVKIR MDTPSGIKDS IPAWIKFSVQ 300 APGEIPYSGI YYDPPEEEKY VFKHPQPKRP KSLRIYESHI GMSSPEPKIN TYVNFRDDVL 360 PRIKRLGYNA VQIMAIQEHS YYASFGYHVT NFFAPSSRFG TPEELKSLID RAHELGLLVL 420 MDIVHSHASN NTLDGLNMFD GTDGHYFHPG SRGYHWMWDS RLFNYGSWEV LRYLLSNARW 480 WLDEYKFDGF RFDGVTSMMY THHGLEVAFT GNYNEYFGFA TDVDAVVYLM LTNDVIHGLF 540 PEAVTIGEDV SGMPTFCLPT QDGGIGFDYR LHMAIADKWI EILKKNDEDW KMGDIIHTLT 600 NRRWLEKCVA YAESHDQALV GDKTIAFWLM DKDMYDFMAL DRPSTPIIDR GIALHKMIRL 660 ITMGLGGEGY LNFMGNEFGH PEWIDFPRGD QHLPNGVVVP GNNNSFDKCR RRFDLGDADY 720 LRYQGMQEFD QAMQHLEEKF GFMTAEHQYI SRKNEGDKII VFERGNLIFV FNFHWTNSYS 780 DYRVGCSTPG KYKIVLDSDD ALFGGFSRLN HAAEYFTSEG WYDDRPRSFL IYAPSRTAVV 840 YALADEAEPA LADATEPEPV DLDDKLLG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 5.0e-8 | 184 | 261 | 84 | + alpha-amylase | ||
PLN03244 | PLN03244 | 1.0e-132 | 269 | 841 | 580 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 126 | 841 | 726 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 316 | 731 | 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 | 269 | 841 | 576 | + 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 | AAT76444.1 | 0 | 1 | 861 | 1 | 855 | starch branching enzyme II [Vigna radiata] |
GenBank | ABO31358.1 | 0 | 1 | 845 | 1 | 840 | starch branching enzyme II-1 [Malus x domestica] |
DDBJ | BAA82348.2 | 0 | 1 | 861 | 1 | 869 | starch branching enzyme [Phaseolus vulgaris] |
EMBL | CAA56319.1 | 0 | 1 | 862 | 1 | 866 | starch branching enzyme I [Pisum sativum] |
EMBL | CBI30261.1 | 0 | 1 | 850 | 1 | 857 | 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 | 3amk_A | 0 | 167 | 851 | 13 | 700 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 167 | 851 | 13 | 700 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 167 | 851 | 13 | 700 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 167 | 851 | 13 | 700 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 0 | 204 | 805 | 6 | 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 |
HO794536 | 681 | 161 | 841 | 0 |
HO777638 | 627 | 215 | 841 | 0 |
HO458123 | 392 | 450 | 841 | 0 |
HO794536 | 79 | 88 | 166 | 2e-19 |
HO777638 | 47 | 170 | 216 | 0.00000000000003 |
Sequence Alignments (This image is cropped. Click for full image.) |
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