y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.009G441800.2 |
Family | GH13 |
Protein Properties | Length: 876 Molecular Weight: 101129 Isoelectric Point: 6.9084 |
Chromosome | Chromosome/Scaffold: 09 Start: 69341058 End: 69349645 |
Description | Alpha amylase family protein |
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 | 420 | 714 | 1.9e-24 |
FNDFTERVLPHVKRAGYNAIQLIGIVEHKDYFTVGYRVTNFFAVSSRYGTPEDFKRLVDEAHGLGLLVFLDIVHSYSAADEMVGLSRFDGSNDCYFHTGK RGHHKYWGTRMFKYSDLDVLHFLLSNLNWWISEYKIDGFHFHSLASMLYTHNGFASFTGDLEEYCNQYVDNDAVKYLILANEILHALHPNIITIAEDATF YPGLCEPTSQGGLGFDYHVNLSASEMWLSLLKNTPDHEWSMSKITSTLLGNKNYADKMLVYAENHNQSISGGQSLAEILLSQGNDKAPQSNELLL |
Full Sequence |
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Protein Sequence Length: 876 Download |
MASLSLQPKF SLHPNNSILH FHPQNKPQII FFTRKVKIKT KTKCSSIDPQ QQQQKQRESF 60 TRKKKSVTET EKGVDPVGFL TKLGITHKAF AQFLRERYKS LKDLKAEIFT RHLNLQEMAS 120 GFEILGTHRH KEHRVDYMDW APGARYCALV GDFNGWSPTT NAAREGLYGH DDYGYWFIIL 180 EDKLREGEEP DELYFQQYNY VDDYDKGDSG VTIDEVFQRA NDEYWEPGED RFIKNRFELP 240 AKLYERLFGP NGPQTLEELG EIPDAETRYK AHKELHKDDP PSNLPPFDVI DNGKEYDIFN 300 VVADPAWQEK FRNKKPPLAY WTEIRKGRKA WLKKYSPAIP HGSKYRVYFN TPDGPLERVP 360 AWATFIQPDA EGKQAYAIHW EPPPEHTYKW KHTAIKPPKS LRIYECHVGI SGSEPKISSF 420 NDFTERVLPH VKRAGYNAIQ LIGIVEHKDY FTVGYRVTNF FAVSSRYGTP EDFKRLVDEA 480 HGLGLLVFLD IVHSYSAADE MVGLSRFDGS NDCYFHTGKR GHHKYWGTRM FKYSDLDVLH 540 FLLSNLNWWI SEYKIDGFHF HSLASMLYTH NGFASFTGDL EEYCNQYVDN DAVKYLILAN 600 EILHALHPNI ITIAEDATFY PGLCEPTSQG GLGFDYHVNL SASEMWLSLL KNTPDHEWSM 660 SKITSTLLGN KNYADKMLVY AENHNQSISG GQSLAEILLS QGNDKAPQSN ELLLRGSSLL 720 KMTKLITFTI GGRGYLNFMG NEFGHPKRVE FPMPSNNFSF SLANRCWDLL EKEGVYQDLF 780 RFDKDMMKLD KNERVLSRGL PNIHHVNDTN MVISYLRGPL LFVFNFHPTD SYERYCIGVD 840 EAGEYQVILN TDERRYGGQG IVKEEQYLQR TISKR* 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02447 | PLN02447 | 5.0e-13 | 90 | 182 | 93 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 2.0e-174 | 384 | 784 | 411 | + 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 | 875 | 875 | + alpha-amylase | ||
PLN03244 | PLN03244 | 0 | 1 | 875 | 882 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 336 | 860 | 534 | + 1,4-alpha-glucan-branching enzyme |
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 |
DDBJ | BAB02827.1 | 0 | 1 | 875 | 1 | 875 | starch-branching enzyme-like protein [Arabidopsis thaliana] |
EMBL | CBI26672.1 | 0 | 1 | 875 | 1 | 868 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_001154629.1 | 0 | 1 | 875 | 1 | 871 | alpha-amylase/ catalytic/ cation binding [Arabidopsis thaliana] |
RefSeq | XP_002278858.1 | 0 | 1 | 875 | 1 | 838 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002529457.1 | 0 | 4 | 875 | 5 | 873 | 1,4-alpha-glucan branching enzyme, putative [Ricinus communis] |
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 | 337 | 862 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 337 | 862 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 337 | 862 | 114 | 650 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
CO104525 | 273 | 385 | 657 | 0 |
BF272517 | 278 | 358 | 635 | 0 |
ES814188 | 271 | 605 | 875 | 0 |
DY965821 | 293 | 267 | 559 | 0 |
JG636329 | 270 | 345 | 614 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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