Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 437417 |
Family | GH13 |
Protein Properties | Length: 799 Molecular Weight: 91533.2 Isoelectric Point: 6.1021 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 269 | 594 | 1.3e-27 |
LPRIKANNYNTVQLMAVMEHSYYASFGYHVTNFFGVSSRSGTPEELKYLIDKAHSLGLRVLMDVVHSHASNNIKDGLNGFDLGQQTQESYFHTGDRGYHK LWDSRLFNYNNWEVERFLLSNLRWWLEEYQFDGFRFDGVTSMLYHHHGIHMSFSGRYRDYFSEASDVDAAVYLMLANELVHTLYPDATTIAEDVSGMPTL GRPVSEGGVGFDYRLAMGIPDTWIKLLKEVTDEHWSMAEIASTLLNRRYTEKAIAYAESHDQSLVGDKTLAFMLMDKEMYAGMSALQEQSIIIERGIALH KMIHFLTMALGGDGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 799 Download |
MEIAIASAVC PAISPCSSSK ERQQQPLRSS RGLLRRSTLV SGQKIMADPR WNFHRSVIKA 60 VKTEEHVARE DLPVVRVDPL LAPHQDHLKY RFSQYERRKR AIEKYEGGLE KFSLGFQKFG 120 FNYEDGYIVY REWAPPAQAA QLIGDFNNWD GWSHPMEKDK YGVWSVRIPD VDGKPGIPHG 180 SRVKFRMQKG DGQWIDRIPA WIKYATVEAG KMGASYDGIL WNPSEDQRYK FEHPRPPKPV 240 VPRIYEAHVG MSSKEPCVAS YIDFADNVLP RIKANNYNTV QLMAVMEHSY YASFGYHVTN 300 FFGVSSRSGT PEELKYLIDK AHSLGLRVLM DVVHSHASNN IKDGLNGFDL GQQTQESYFH 360 TGDRGYHKLW DSRLFNYNNW EVERFLLSNL RWWLEEYQFD GFRFDGVTSM LYHHHGIHMS 420 FSGRYRDYFS EASDVDAAVY LMLANELVHT LYPDATTIAE DVSGMPTLGR PVSEGGVGFD 480 YRLAMGIPDT WIKLLKEVTD EHWSMAEIAS TLLNRRYTEK AIAYAESHDQ SLVGDKTLAF 540 MLMDKEMYAG MSALQEQSII IERGIALHKM IHFLTMALGG DGYLNFMGNE FGHPEWIDFP 600 REGNKWSYDK CRRQWDLVDT DHLRYKFMNE FDKAMNALEE KYHFLTLPLI VSSAHDKDKV 660 IVFERGDLVF VFNFHPETTY EGYKIGCDLP GKYKIALDSD AFDFGGRGRV GHDVDHFTSP 720 EGIPGRPETN FNNRPSSFLV LSPARTCQVY FKVPEDAVQS EEENEEPAAS VLQLISQSAA 780 QKDLPFNFMD DIPDFSQD* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 7.0e-7 | 85 | 171 | 93 | + alpha-amylase | ||
PLN03244 | PLN03244 | 4.0e-135 | 175 | 750 | 583 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 70 | 762 | 694 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 225 | 633 | 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 | 175 | 750 | 579 | + alpha-amylase |
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 | 16 | 772 | 31 | 793 | starch branching enzyme I [Populus trichocarpa] |
DDBJ | BAE96955.1 | 0 | 14 | 793 | 36 | 819 | starch branching enzyme I [Ipomoea batatas] |
EMBL | CAA54308.1 | 0 | 8 | 755 | 15 | 777 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 23 | 784 | 37 | 809 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 23 | 784 | 14 | 786 | PREDICTED: hypothetical protein [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 | 72 | 756 | 11 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 72 | 756 | 11 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 72 | 756 | 11 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 72 | 756 | 11 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 7e-39 | 133 | 706 | 32 | 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 | 611 | 158 | 766 | 0 |
HO794536 | 710 | 74 | 770 | 0 |
HO777638 | 656 | 128 | 770 | 0 |
HO458123 | 404 | 362 | 753 | 0 |
HO458123 | 404 | 362 | 753 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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