y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.002G241400.1 |
Family | GH13 |
Protein Properties | Length: 871 Molecular Weight: 99638 Isoelectric Point: 4.8926 |
Chromosome | Chromosome/Scaffold: 02 Start: 60479036 End: 60489562 |
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 | |||
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Family | Start | End | Evalue |
GH13 | 345 | 665 | 2.5e-29 |
LPRIKRLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPDDLKSLIDKAHELGILVLMDIVHSHASNNVLDGLNMFDGTDGHYFHTGSRGHHSVWD SRLFNYGSWEVLRYLLSNARWWLEEYKFDGYRFDGVTSMMYIHHGLQVGFTGNYNEYFGYATDVDAVVYLMLVNDMIHGLYPEAVTIGEDVSGMPTFCIP VQDGGVGFDYRLHMAIADKWIEILKKRDEDWKMGEIVHTLTNRRWMEKCVAYAESHDQALVGDKTIAFWLMDKDMYEFMALDRPSTALIDRGIALHKMIR LVTMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 871 Download |
MVYSVSDLRL PCSPSVYSFS QSSFNASRRS SSFSLLLKKD LFSRKIFAQK SSYDSDSSPL 60 TVASKKVLVP DDQGEGASSL TDELESPSTI SDDPQVIHDV ESEEMEDDTK IEVEEQESAP 120 KELSTPLKRK ISTEKSEAKP RTIPPPGIGQ KIYEIDPSLL DFRQHLDYRY AQYKRMREEI 180 DKYEGGLEVF SRGYEKLGFI GSEMGITYRE WAPGAKSAAL IGDFNNWNPN ADIMNRNEFG 240 VWEIFLPNNA DGSPAIPHGS RVKIRMETPS GIKDSIPAWI KFSVQAPGEI PYNGIYYDPP 300 EEEKYVFKHP RPQRPKSLRI YESHVGMSSP EPMINTYANF RDDVLPRIKR LGYNAVQIMA 360 IQEHSYYASF GYHVTNFFAP SSRFGTPDDL KSLIDKAHEL GILVLMDIVH SHASNNVLDG 420 LNMFDGTDGH YFHTGSRGHH SVWDSRLFNY GSWEVLRYLL SNARWWLEEY KFDGYRFDGV 480 TSMMYIHHGL QVGFTGNYNE YFGYATDVDA VVYLMLVNDM IHGLYPEAVT IGEDVSGMPT 540 FCIPVQDGGV GFDYRLHMAI ADKWIEILKK RDEDWKMGEI VHTLTNRRWM EKCVAYAESH 600 DQALVGDKTI AFWLMDKDMY EFMALDRPST ALIDRGIALH KMIRLVTMGL GGEGYLNFMG 660 NEFGHPEWID FPRGDQRLPN GVVIPGNGYS YDKCRRRFDL GDADYLRYRG MQEFDQAMQH 720 VEEKYGFMTS EHTYISRKDE KDRVIVFERG NLVFVFNFHW NNSYFDYRVG CAKPGKYKIV 780 LDSDDPLFGG FGRLDHNAEY FSFEGWFDDR PRSFMVYAPN RTAVVYALVE DEPKVVNDLE 840 LVEIPETVKP AAAEPVKESE PDEESEPLDS * 900 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 6.0e-10 | 162 | 246 | 91 | + alpha-amylase | ||
PLN03244 | PLN03244 | 4.0e-136 | 254 | 828 | 583 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 78 | 838 | 765 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 301 | 716 | 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 | 254 | 829 | 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 |
GenBank | AAT76444.1 | 0 | 1 | 855 | 1 | 856 | starch branching enzyme II [Vigna radiata] |
GenBank | ABN05322.1 | 0 | 1 | 832 | 1 | 827 | starch branching enzyme II [Populus trichocarpa] |
GenBank | ABO31358.1 | 0 | 1 | 834 | 1 | 844 | starch branching enzyme II-1 [Malus x domestica] |
DDBJ | BAA82348.2 | 0 | 1 | 855 | 1 | 870 | starch branching enzyme [Phaseolus vulgaris] |
RefSeq | XP_002534111.1 | 0 | 1 | 840 | 2 | 848 | starch branching enzyme II, 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 | 152 | 832 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 152 | 832 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 152 | 832 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 152 | 832 | 13 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3k1d_A | 0 | 92 | 824 | 31 | 717 | A Chain A, Crystal Structure Of Glycogen Branching Enzyme Synonym: 1,4- Glucan:1,4-Alpha-D-Glucan 6-Glucosyl-Transferase From Mycob Tuberculosis H3 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 710 | 146 | 850 | 0 |
HO777638 | 656 | 200 | 850 | 0 |
HO458123 | 395 | 435 | 829 | 0 |
HO458123 | 306 | 138 | 434 | 0 |
HO777638 | 46 | 155 | 200 | 0.0000000009 |
Sequence Alignments (This image is cropped. Click for full image.) |
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