Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_10430611g0010 |
Family | GH13 |
Protein Properties | Length: 656 Molecular Weight: 75113.3 Isoelectric Point: 8.2018 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH13 | 308 | 620 | 1.4e-27 |
LPRIKANNYNTVQLMAVAEHSYYGSFGYHVTNLFAPSSRSGTPEDLKFLIEKAHSLGLRVLMDMVHSHASNNVTDGLNGYDIGQRTEESYFHTGERGYHK LWDSRLFNYGNWEVQRFLLSNLRWWLEEFQFDGFRFDGVTSMLYHHHGINVGFTGNYQEYFGKQTDVDAIAYLMLANSLIRNIYPDATVIAEDVSGMPTL GRPISEGGLGFDYRLAMAIPDKWIEYLKHKLDEQWSMKEIVLTLTNRRYTEKCVAYAESHDQAIVGDKTIAFSLMDKEMYSAMSCLQSPSPVIDRGIALH KMIHFITLALGGE |
Full Sequence |
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Protein Sequence Length: 656 Download |
MQGSTLALGF GLGVGPSDVN LSWGCGRHCH CHSKNPERTQ FSSKQDSRWH SNSSKCLLRK 60 DLPQNLHTLL NGRVWQIPKF PARRRIFIAH STLKNNKSTM NITIEDELEN LGVLNVDPSL 120 ASHKAHLQYR YSKYLQQKQT IEKYEGSLED FSKGYLKYGF NREGNKIVYR EWAPAAKEAQ 180 LIGDFNAWNG SCHRMERDQF GVWTVYIPDK DGKPAIPHGS KVKFRMKIAN GTWIDRIPAW 240 IRYATVDPSN FGAAYDGVYW DPPPSKRYKF KYPRPPKPEA PRIYEAHVGM SGIEPRVASY 300 VEFAENVLPR IKANNYNTVQ LMAVAEHSYY GSFGYHVTNL FAPSSRSGTP EDLKFLIEKA 360 HSLGLRVLMD MVHSHASNNV TDGLNGYDIG QRTEESYFHT GERGYHKLWD SRLFNYGNWE 420 VQRFLLSNLR WWLEEFQFDG FRFDGVTSML YHHHGINVGF TGNYQEYFGK QTDVDAIAYL 480 MLANSLIRNI YPDATVIAED VSGMPTLGRP ISEGGLGFDY RLAMAIPDKW IEYLKHKLDE 540 QWSMKEIVLT LTNRRYTEKC VAYAESHDQA IVGDKTIAFS LMDKEMYSAM SCLQSPSPVI 600 DRGIALHKMI HFITLALGGE GYLNFMGNEV YTDIHPFIIV SYQKSNTCIL FTMMTE 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 8.0e-9 | 122 | 210 | 98 | + alpha-amylase | ||
PLN03244 | PLN03244 | 4.0e-99 | 214 | 629 | 420 | + alpha-amylase; Provisional | ||
PLN02960 | PLN02960 | 8.0e-132 | 214 | 629 | 417 | + alpha-amylase | ||
PLN02447 | PLN02447 | 0 | 102 | 629 | 528 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 279 | 629 | 351 | + 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. |
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 | 83 | 629 | 65 | 610 | starch branching enzyme I [Populus trichocarpa] |
EMBL | CAA54308.1 | 0 | 77 | 629 | 57 | 611 | 1,4-alpha-glucan branching enzyme [Manihot esculenta] |
EMBL | CBI18866.1 | 0 | 89 | 629 | 74 | 614 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284841.1 | 0 | 89 | 629 | 51 | 591 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002307789.1 | 0 | 103 | 629 | 3 | 529 | predicted protein [Populus trichocarpa] |
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 | 102 | 629 | 2 | 529 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 102 | 629 | 2 | 529 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 102 | 629 | 2 | 529 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3aml_A | 0 | 102 | 629 | 2 | 529 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 1m7x_D | 3.99931e-42 | 172 | 577 | 32 | 424 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO619167 | 434 | 197 | 629 | 0 |
HO794536 | 518 | 113 | 629 | 0 |
HO777638 | 464 | 167 | 629 | 0 |
DV996662 | 287 | 1 | 287 | 0 |
HO777638 | 47 | 116 | 162 | 0.0007 |
Sequence Alignments (This image is cropped. Click for full image.) |
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