| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.009G406400.2 |
| Family | GH13 |
| Protein Properties | Length: 782 Molecular Weight: 89688 Isoelectric Point: 5.4859 |
| Chromosome | Chromosome/Scaffold: 09 Start: 59754748 End: 59774698 |
| Description | starch branching enzyme 2.2 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH13 | 278 | 599 | 1e-29 |
| LPRIKRLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPDDLKSLIDRAHELGLLVLMDIVHSHASNNVLDGLNMFDGTDAHYFHSGSKGHHWMWD SRLFNYGSWEVLRFLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVAFTGNYNEYFGYATDVEAVVYLMLVNDMIHGLYPEAVTIGEDVSGMPTFCLP VQDGGVGFDYRLHMAVADKWIELLKKRDEDWKMGDIVYTLVNRRWLEKCVVYAESHDQALVGDKTIAFWLMDKDMYDFMSLDRPSSPIIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGHP | |||
| Full Sequence |
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| Protein Sequence Length: 782 Download |
| MTDQLESPST ISDDPQVIHN VDIEGMEDDK MIAVEEQESF PSVFANSDEE AHAEEPSVPL 60 HRNASTEKSE AKPRSIPPPG EGQKIYEIDS LLLGFRNHID YRYAQYKKIR KEIDKYEGGL 120 EVFSRGYEKL GFTRSETGIT YREWAPGAKS AALIGDFNNW NPSADTMSQN EFGVWEIFLP 180 NTADGSPAIP HGSRVKIRME TRSGVKDSIP AWIKFSVQAP GEIPYSGIYY DPPEEEKYVF 240 KHPHPKRPKS LRIYESHVGM SSMEPLINTY ANFRDNVLPR IKRLGYNAVQ IMAIQEHSYY 300 ASFGYHVTNF FAPSSRFGTP DDLKSLIDRA HELGLLVLMD IVHSHASNNV LDGLNMFDGT 360 DAHYFHSGSK GHHWMWDSRL FNYGSWEVLR FLLSNARWWL EEYKFDGFRF DGVTSMMYTH 420 HGLQVAFTGN YNEYFGYATD VEAVVYLMLV NDMIHGLYPE AVTIGEDVSG MPTFCLPVQD 480 GGVGFDYRLH MAVADKWIEL LKKRDEDWKM GDIVYTLVNR RWLEKCVVYA ESHDQALVGD 540 KTIAFWLMDK DMYDFMSLDR PSSPIIDRGI ALHKMIRLIT MGLGGEGYLN FMGNEFGHPE 600 WIDFPRGEQH LPSGKVIPGN NFSYDKCRRR FDLGDADYLR YKGMQQFDQA MQHVEAKYGF 660 MTSEHQYISR KDEGERVIVF ERGNLVFVFN FHWHESYGGY RVGCSKPGKY KIVLDSDDLL 720 FGGFNRLNHD VEFFSTEGWY DNRPRSLLVY APNRTAVVYA LVEDEPKATG NLQLTENVKN 780 C* 840 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02960 | PLN02960 | 6.0e-10 | 102 | 179 | 84 | + alpha-amylase | ||
| PLN03244 | PLN03244 | 3.0e-137 | 187 | 761 | 588 | + alpha-amylase; Provisional | ||
| PLN02447 | PLN02447 | 0 | 41 | 765 | 731 | + 1,4-alpha-glucan-branching enzyme | ||
| cd11321 | AmyAc_bac_euk_BE | 0 | 234 | 649 | 417 | + 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 | 187 | 762 | 579 | + alpha-amylase | ||
| Gene Ontology | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ABN05322.1 | 0 | 12 | 765 | 90 | 827 | starch branching enzyme II [Populus trichocarpa] |
| EMBL | CBI30261.1 | 0 | 2 | 760 | 82 | 849 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002277213.1 | 0 | 2 | 760 | 291 | 1058 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002326414.1 | 0 | 49 | 765 | 8 | 724 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002534111.1 | 0 | 3 | 780 | 93 | 852 | starch branching enzyme II, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3amk_A | 0 | 85 | 765 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3aml_A | 0 | 85 | 765 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
| PDB | 3vu2_B | 0 | 85 | 765 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 3vu2_A | 0 | 85 | 765 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
| PDB | 1m7x_D | 0 | 125 | 728 | 9 | 582 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HO794536 | 689 | 79 | 766 | 0 |
| HO777638 | 633 | 135 | 766 | 0 |
| HO458123 | 395 | 368 | 762 | 0 |
| HO458123 | 304 | 71 | 367 | 0 |
| HO777638 | 47 | 88 | 134 | 0.0000003 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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