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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s15_181V6.2 |
Family | GH13 |
Protein Properties | Length: 793 Molecular Weight: 90472.2 Isoelectric Point: 6.3782 |
Chromosome | Chromosome/Scaffold: 15 Start: 1173286 End: 1180286 |
Description | starch branching enzyme 2.1 |
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 | 305 | 630 | 7.7e-27 |
LPRIKANNYNTIQLMAIMEHAYYGCFGYHVTNFFAASSRCGTPEDLKYLIDKAHSMGLRVLMDVVHSHASTNAVDGLAGYDLGQSSQESYFHTGARGYHT LWDSRLFNYGSWEVQRFLLSNLRWWMDEYKFDGFRFDGVTSMLYHHHGLNMCFTGNYHEYFSEATDVEAVMYLMLANELVHKLLPDATVIAEDVSGMPTL CRSVEEGGVGFDYRLAMAIPDKWIQYLKERKDEDWSMGDIVYTLTNRRYTEPCVGYAESHDQSMVGDKTFAFLLMDKEMYFSMTATQPANLIVDRGIALH KMIHFITMALGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 793 Download |
MLAVPACHGR SSPAATHASL QSSSQVEGRG ITSSDVLGWQ RLTLKRSMWG VGGLSRSLNF 60 KSSSPPTVRA TSIKTEKTEK PDKPAKSAEP AEPAQLAGWK DLNGMEKLGV VEVDPMLAPH 120 QNHLRYRYRE FLKRKMEIEK VEGSLENFAK GYDKFGFTRD GDCIVYQEWA PAAAAAQLIG 180 DFNNWDGSNH KMERDEFGVW SIRLPDEDGV PAIPHGSKVK FRMQKGDGTW VDRIPAWIKY 240 AVVDPNVFAA YYDGVYWDPP AEEKYEFKHA RPPKPAAPLI YEAHVGMSSK EPVVASYRQF 300 ADEVLPRIKA NNYNTIQLMA IMEHAYYGCF GYHVTNFFAA SSRCGTPEDL KYLIDKAHSM 360 GLRVLMDVVH SHASTNAVDG LAGYDLGQSS QESYFHTGAR GYHTLWDSRL FNYGSWEVQR 420 FLLSNLRWWM DEYKFDGFRF DGVTSMLYHH HGLNMCFTGN YHEYFSEATD VEAVMYLMLA 480 NELVHKLLPD ATVIAEDVSG MPTLCRSVEE GGVGFDYRLA MAIPDKWIQY LKERKDEDWS 540 MGDIVYTLTN RRYTEPCVGY AESHDQSMVG DKTFAFLLMD KEMYFSMTAT QPANLIVDRG 600 IALHKMIHFI TMALGGEGYL NFMGNEFGHP EWIDFPRQGN NWSFDKCRRR WDLVDQDHLR 660 YKFMNNFNRA MIALEEEFQF VSSRKQYISC QHEYDKLIVF ERGDLVFVFN FHPTNTYSGL 720 KVGCEIPGKY RICLDSDAAE FGGHSRVDHN VDHFTSPEGE PGRPETNYNN RPHSFMVMAP 780 SRSCQVYYKV PE* 840 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 3.0e-8 | 121 | 206 | 92 | + alpha-amylase | ||
PLN03244 | PLN03244 | 7.0e-140 | 210 | 787 | 583 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 104 | 792 | 689 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 262 | 669 | 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 | 210 | 788 | 580 | + 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 |
EMBL | CAA54308.1 | 0 | 105 | 792 | 90 | 777 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 106 | 792 | 94 | 780 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_001754772.1 | 0 | 105 | 792 | 1 | 688 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001762321.1 | 0 | 105 | 786 | 1 | 682 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001763855.1 | 0 | 105 | 792 | 1 | 688 | predicted protein [Physcomitrella patens subsp. patens] |
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 | 105 | 792 | 8 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3amk_A | 0 | 105 | 792 | 8 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 105 | 792 | 8 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 105 | 792 | 8 | 695 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 5.99756e-43 | 166 | 743 | 29 | 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 | 600 | 194 | 792 | 0 |
HO794536 | 690 | 110 | 787 | 0 |
HO777638 | 636 | 164 | 787 | 0 |
HO458123 | 404 | 398 | 790 | 0 |
HO777638 | 47 | 113 | 159 | 0.007 |
Sequence Alignments (This image is cropped. Click for full image.) |
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