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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 165481 |
Family | GH13 |
Protein Properties | Length: 783 Molecular Weight: 90720.6 Isoelectric Point: 5.1594 |
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 | 324 | 627 | 6.2e-22 |
QEVLPHVKKCGYNVVQLMGVQEHVDYSSVGYKMTNQFAVSSRFGTPEDFKFLVDTAHGLGLLVFMDIVHSHVAPDEVCGLAMFDGANDCFLHYGEHEVKR FLLSNLKWWVEEYRIDGFYFHSVGSMLYTHNGFANFTGSLDEYCNQYVDMDAHIYLILANELLHNLTPRIITIAEDATLFPGLCASHEQGGFGFDYYVST APSDMWLYLIEKVPLEEWSVKQIAESLLKLSESDGKALVYVENHSQSISGGKSLFQALIEKNVEYPDAVNMLKSVSMIKMIKLLTASLGGSAYLTFMGNE FGHT |
Full Sequence |
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Protein Sequence Length: 783 Download |
MEIKRKFFHR YDILGMRHHF FHYVEYFEWA PGATSCSLIG DFNNWDCTKN RAEKGYFGRD 60 DYGTWRITVE DKLREGQEKD PHWQEYNYSV EYDRGDGDID IEALYQKMED EYWEPGEDQY 120 LKDTRPFEEA LFKSIFGENF GCIKVGKEEE VNELAYNTED EETMDYSKFP PGYEEWVKKT 180 DQAHLPPLKQ DPTRYSEPTV VDDPVWRERV LAKKPPLPIW EYTVKGFKAW EKKYLPAIPH 240 GSRVRVYFKT PEGPVERVPA WAKYVLPDPD GKMWSAVYWE PPIQERHQWQ HERPKPPKSL 300 RIYECHVGMS SEEAGISTFK RFSQEVLPHV KKCGYNVVQL MGVQEHVDYS SVGYKMTNQF 360 AVSSRFGTPE DFKFLVDTAH GLGLLVFMDI VHSHVAPDEV CGLAMFDGAN DCFLHYGEHE 420 VKRFLLSNLK WWVEEYRIDG FYFHSVGSML YTHNGFANFT GSLDEYCNQY VDMDAHIYLI 480 LANELLHNLT PRIITIAEDA TLFPGLCASH EQGGFGFDYY VSTAPSDMWL YLIEKVPLEE 540 WSVKQIAESL LKLSESDGKA LVYVENHSQS ISGGKSLFQA LIEKNVEYPD AVNMLKSVSM 600 IKMIKLLTAS LGGSAYLTFM GNEFGHTERV EFPRATNNFS YEFARRRWSL LDDKWHAKLA 660 EFDNALMAIE QKYLFLNSNA PATNLQVDDS SKTVVFTRDN LIFAYNFHPR KSADEYEILV 720 DEPGQYELLL DTDDVKYGGM GRLKTKQKRI DVFSMKLSLT LPQLSAQVYR LAKIWDAAVS 780 VM* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 1.0e-9 | 26 | 71 | 46 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 1.0e-156 | 284 | 663 | 405 | + 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 | 1 | 777 | 818 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 5 | 774 | 803 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 236 | 780 | 584 | + 1,4-alpha-glucan-branching enzyme |
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 | 236 | 743 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0.0005 | 26 | 95 | 69 | 131 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 236 | 743 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0.0006 | 26 | 95 | 69 | 131 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 236 | 743 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
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 |
Sequence Alignments (This image is cropped. Click for full image.) |
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