y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.009G406400.5 |
Family | GH13 |
Protein Properties | Length: 584 Molecular Weight: 67456.4 Isoelectric Point: 6.2076 |
Chromosome | Chromosome/Scaffold: 09 Start: 59759588 End: 59775348 |
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 | 80 | 401 | 2.5e-30 |
LPRIKRLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRFGTPDDLKSLIDRAHELGLLVLMDIVHSHASNNVLDGLNMFDGTDAHYFHSGSKGHHWMWD SRLFNYGSWEVLRFLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLQVAFTGNYNEYFGYATDVEAVVYLMLVNDMIHGLYPEAVTIGEDVSGMPTFCLP VQDGGVGFDYRLHMAVADKWIELLKKRDEDWKMGDIVYTLVNRRWLEKCVVYAESHDQALVGDKTIAFWLMDKDMYDFMSLDRPSSPIIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGHP |
Full Sequence |
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Protein Sequence Length: 584 Download |
METRSGVKDS IPAWIKFSVQ APGEIPYSGI YYDPPEEEKY VFKHPHPKRP KSLRIYESHV 60 GMSSMEPLIN TYANFRDNVL PRIKRLGYNA VQIMAIQEHS YYASFGYHVT NFFAPSSRFG 120 TPDDLKSLID RAHELGLLVL MDIVHSHASN NVLDGLNMFD GTDAHYFHSG SKGHHWMWDS 180 RLFNYGSWEV LRFLLSNARW WLEEYKFDGF RFDGVTSMMY THHGLQVAFT GNYNEYFGYA 240 TDVEAVVYLM LVNDMIHGLY PEAVTIGEDV SGMPTFCLPV QDGGVGFDYR LHMAVADKWI 300 ELLKKRDEDW KMGDIVYTLV NRRWLEKCVV YAESHDQALV GDKTIAFWLM DKDMYDFMSL 360 DRPSSPIIDR GIALHKMIRL ITMGLGGEGY LNFMGNEFGH PEWIDFPRGE QHLPSGKVIP 420 GNNFSYDKCR RRFDLGDADY LRYKGMQQFD QAMQHVEAKY GFMTSEHQYI SRKDEGERVI 480 VFERGNLVFV FNFHWHESYG GYRVGCSKPG KYKIVLDSDD LLFGGFNRLN HDVEFFSTEG 540 WYDNRPRSLL VYAPNRTAVV YALVEDEPKA TGNLQLTENV KNC* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0296 | GlgB | 3.0e-98 | 1 | 563 | 573 | + 1,4-alpha-glucan branching enzyme [Carbohydrate transport and metabolism] | ||
PLN03244 | PLN03244 | 4.0e-134 | 3 | 563 | 574 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 1 | 567 | 571 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 36 | 451 | 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 | 3 | 564 | 565 | + alpha-amylase |
Gene Ontology | |
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GO Term | Description |
GO:0003824 | catalytic activity |
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 | 567 | 266 | 832 | starch branching enzyme II [Vigna radiata] |
GenBank | ABN05322.1 | 0 | 1 | 567 | 261 | 827 | starch branching enzyme II [Populus trichocarpa] |
DDBJ | BAA82348.2 | 0 | 1 | 568 | 281 | 849 | starch branching enzyme [Phaseolus vulgaris] |
EMBL | CAA56319.1 | 0 | 1 | 582 | 282 | 861 | starch branching enzyme I [Pisum sativum] |
RefSeq | XP_002534111.1 | 0 | 1 | 582 | 274 | 852 | 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 | 9 | 567 | 135 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 9 | 567 | 135 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 9 | 567 | 135 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 9 | 567 | 135 | 696 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 2e-40 | 53 | 530 | 132 | 582 | 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 |
HO777638 | 569 | 1 | 568 | 0 |
HO794536 | 569 | 1 | 568 | 0 |
HO458123 | 395 | 170 | 564 | 0 |
HO458123 | 169 | 1 | 169 | 0 |
HO619167 | 583 | 9 | 578 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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