Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.009G011000.1 |
Family | GH13 |
Protein Properties | Length: 848 Molecular Weight: 96261.1 Isoelectric Point: 5.5714 |
Chromosome | Chromosome/Scaffold: 09 Start: 1776410 End: 1783521 |
Description | starch branching enzyme 2.2 |
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 | 286 | 611 | 1.2e-28 |
LPRIRANNYNTVQLMAGMEHSYYASFGYHVTNFYAVSSRSGTPEDLKYLIDKAHSLGLQVLMDVIHSHASNNITDGLNGFDVGQTSQDSYFHTGDRGYHK LWDSRLFNYANWEVLRFLLSNLRWWLEEFEFDGFRFDGITSMLYHHHGINIAFTGDYNEYFSEATDVDAVVYLMLANCLIHSILPDATVIAEDVSGMPGI GHQVSGGGIGFDYRLAMAIPDKWIDYLKNKNEYSWSMKEISWSLTNRRYTEKCVSYAESHDQAIVGDKTVAFLLMDEEMYSGMSCLVDASPIVERGIALQ KMIHFITMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 848 Download |
MFNCLCLNPF ISVSSTIACT IHTVRSRQHL APQKSVDLAV GYRNPLGYGF GSGLRRSLHE 60 MVSSRFKGVA VMTDDKSTIS STEEYLENIG IFSIDPSLKP YKDHFKYRLK RYVEQKKLIE 120 EYEGGLEEFA KGYLKFGFNR EEGGIVYREW APAAQEAQII GDFNGWDGSN HQMEKDQFGV 180 WSIKIPDVDG NPAIPHSSRV KFRFRHGDGV WVDRIPAWIK YATVDPTRFA APYDGVYWDP 240 PLSERYQFKY PRPPKPKAPR IYEAHVGMSS SEPRINSYRE FADEILPRIR ANNYNTVQLM 300 AGMEHSYYAS FGYHVTNFYA VSSRSGTPED LKYLIDKAHS LGLQVLMDVI HSHASNNITD 360 GLNGFDVGQT SQDSYFHTGD RGYHKLWDSR LFNYANWEVL RFLLSNLRWW LEEFEFDGFR 420 FDGITSMLYH HHGINIAFTG DYNEYFSEAT DVDAVVYLML ANCLIHSILP DATVIAEDVS 480 GMPGIGHQVS GGGIGFDYRL AMAIPDKWID YLKNKNEYSW SMKEISWSLT NRRYTEKCVS 540 YAESHDQAIV GDKTVAFLLM DEEMYSGMSC LVDASPIVER GIALQKMIHF ITMALGGEGY 600 LNFMGNEFGH PEWIDFPREG NGWSYEKCRR QWNLVDTDHL RYKFMNAFDR AMNLLDDKFS 660 FLKSTKQIVS SAHDEDKVIV FERGDLIFVF NFHPENTYEG YKVGCDLPGK YRVALDSDAW 720 KFGGHGRVGH GVDHFTSPEG IPGVPETNFN NRPNSFKVLS PARTCVVYYR VDENQEGSND 780 SLVGLEDTFA AADVAKIPDK SASIESEYSN NLDGVKETST SAQISVESEV INLDKVGIVA 840 ASLDREI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 1.0e-7 | 108 | 188 | 87 | + alpha-amylase | ||
PLN03244 | PLN03244 | 3.0e-118 | 192 | 768 | 581 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 8.0e-164 | 192 | 769 | 585 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 69 | 784 | 716 | + 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. |
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 | 847 | 1 | 847 | starch branching enzyme [Phaseolus vulgaris] |
EMBL | CAA54308.1 | 0 | 1 | 830 | 1 | 821 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CAA56320.1 | 0 | 22 | 831 | 8 | 823 | starch branching enzyme II [Pisum sativum] |
EMBL | CBI18866.1 | 0 | 5 | 796 | 7 | 805 | 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 | 84 | 776 | 6 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 84 | 776 | 6 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 84 | 776 | 6 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 84 | 776 | 6 | 698 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3k1d_A | 3.00018e-42 | 144 | 766 | 137 | 717 | A Chain A, Crystal Structure Of Glycogen Branching Enzyme Synonym: 1,4- Glucan:1,4-Alpha-D-Glucan 6-Glucosyl-Transferase From Mycob Tuberculosis H3 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO619167 | 668 | 175 | 831 | 0 |
HO794536 | 695 | 91 | 773 | 0 |
HO781588 | 385 | 465 | 848 | 0 |
HO777638 | 643 | 143 | 773 | 0 |
HO777638 | 47 | 94 | 140 | 0.016 |
Sequence Alignments (This image is cropped. Click for full image.) |
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