Basic Information | |
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Species | Carica papaya |
Cazyme ID | evm.model.supercontig_5.62 |
Family | GH13 |
Protein Properties | Length: 909 Molecular Weight: 103159 Isoelectric Point: 4.7214 |
Chromosome | Chromosome/Scaffold: 5 Start: 484692 End: 501706 |
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 | 392 | 712 | 2.6e-29 |
LPRIKRLGYNAVQIMAIQEHSYYASFGYHVTNFFAPSSRCGTPDDLKSLVDRAHELGLIVLMDVVHSHASNNTLDGLNMFDGTDGHYFHTGSQGYHWMWD SRLFNYGSWEVLRFLLSNARWWLEEYKFDGFRFDGVTSMMYTHHGLAVGFTGNYKEYFGFATDVDAVVYLMLVNDLIHGLFPEAVTVGEDVSGMPTFCIP VQDGGVGFDYRLHMAVPDKWIELLKKKDEDWRMGDIVYTLTNRRWLEKCVAYAESHDQALVGDKTIAFWLMDKDMYDFMALDRPSTPLIDRGIALHKMIR LITMGLGGEGYLNFMGNEFGH |
Full Sequence |
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Protein Sequence Length: 909 Download |
MVYSSVSGIR FPSAILLHNS SPSSFSGDRR SATLSLFLKK EPLFRKIFAR KPSYDSDSPS 60 LVVTASEKVL VPGSQSDGSS SMTDQLEVPE TLSEDSQVLD NVDAQTVENG EVEDEEPDTV 120 SSSFVDDSDK PLVKESVPVG GRVTLEEMEA RPKSIPSSFV DDSDKPLVKE SVPVGGRVTL 180 EEMEARPKSI PPPGTGQKIY EIDPMLNGYR DHLEYRYEQY KKMREAIDKY EGGLEVFSRG 240 YEKLGFLRSA TGITYREWAP GAKSASLIGD FNNWNPHADV MTQNEFGVWE IFLPNSVDGS 300 PPIPHGSRVK IRMDTPSGIK DSIPAWIKFS VQAPGEIPYN GIYYDPPEEE KYVFVHPRPK 360 RPKSLRIYES HVGMSSTEPI VNTYANFRDD VLPRIKRLGY NAVQIMAIQE HSYYASFGYH 420 VTNFFAPSSR CGTPDDLKSL VDRAHELGLI VLMDVVHSHA SNNTLDGLNM FDGTDGHYFH 480 TGSQGYHWMW DSRLFNYGSW EVLRFLLSNA RWWLEEYKFD GFRFDGVTSM MYTHHGLAVG 540 FTGNYKEYFG FATDVDAVVY LMLVNDLIHG LFPEAVTVGE DVSGMPTFCI PVQDGGVGFD 600 YRLHMAVPDK WIELLKKKDE DWRMGDIVYT LTNRRWLEKC VAYAESHDQA LVGDKTIAFW 660 LMDKDMYDFM ALDRPSTPLI DRGIALHKMI RLITMGLGGE GYLNFMGNEF GHPEWIDFPR 720 GDQKLPNGSV IPGNNYSYDK CRRRFDLGDA NYLRYCGMQE FDQAMQHLEE KYGFMTSEHQ 780 YVSRMDEGDR MIVFERGNLV FVFNFHWTKS YSGYRVGCLK PGKYKIVLDS DDALFGGFSR 840 LERNAEYFTS EGSYNDRPCS FMVYAPSRTA VVYALIDDEE KKGGEKEKEN EEEEDNGEGE 900 EEEEAVKE* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02960 | PLN02960 | 2.0e-8 | 213 | 293 | 87 | + alpha-amylase | ||
PLN03244 | PLN03244 | 8.0e-137 | 301 | 875 | 590 | + alpha-amylase; Provisional | ||
PLN02447 | PLN02447 | 0 | 138 | 876 | 745 | + 1,4-alpha-glucan-branching enzyme | ||
cd11321 | AmyAc_bac_euk_BE | 0 | 348 | 763 | 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 | 301 | 875 | 579 | + 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 | ABO31358.1 | 0 | 4 | 881 | 3 | 844 | starch branching enzyme II-1 [Malus x domestica] |
GenBank | ACA35286.1 | 0 | 1 | 887 | 1 | 881 | starch branching enzyme I [Cucumis sativus] |
DDBJ | BAA82348.2 | 0 | 1 | 880 | 1 | 848 | starch branching enzyme [Phaseolus vulgaris] |
EMBL | CBI30261.1 | 0 | 1 | 874 | 1 | 849 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002277213.1 | 0 | 36 | 874 | 244 | 1058 | PREDICTED: hypothetical protein [Vitis vinifera] |
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 | 199 | 882 | 13 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3aml_A | 0 | 199 | 884 | 13 | 704 | A Chain A, Structure Of The Starch Branching Enzyme I (Bei) From Oryza Sativa L |
PDB | 3vu2_B | 0 | 199 | 882 | 13 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 3vu2_A | 0 | 199 | 882 | 13 | 699 | A Chain A, Structure Of The Starch Branching Enzyme I (bei) Complexed With Maltopentaose From Oryza Sativa L |
PDB | 1m7x_D | 9.80909e-45 | 239 | 837 | 9 | 577 | A Chain A, The X-Ray Crystallographic Structure Of Branching Enzyme |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
starch biosynthesis | RXN-7710 | EC-2.4.1.18 | 1,4-α-glucan branching enzyme |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO794536 | 683 | 193 | 875 | 0 |
HO777638 | 629 | 247 | 875 | 0 |
HO458123 | 395 | 482 | 876 | 0 |
HO458123 | 304 | 185 | 481 | 0 |
HO777638 | 47 | 202 | 248 | 0.00000002 |
Sequence Alignments (This image is cropped. Click for full image.) |
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