Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna12648.1-v1.0-hybrid |
Family | AA7 |
Protein Properties | Length: 515 Molecular Weight: 57298.3 Isoelectric Point: 4.9511 |
Chromosome | Chromosome/Scaffold: 1 Start: 5568474 End: 5571097 |
Description | cytokinin oxidase 2 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 53 | 247 | 9.2e-26 |
DWGHIFHEYAAAVLYPNSTNDIATLLQFANNGSTTFGIAARGQGHSARGQAMAKDGIVINMTTLNNMGSRIVVSQSGEYADVGGEQLWIDVLRATVDQGL SPVSWTDYLYLSVGGTLSNAGISGQTFRYGPQITNVYELDVVTGKGDVITCSSKQTSELFYSALGGLGQVGIITRARIALQPAPNRAVWIRLFYS |
Full Sequence |
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Protein Sequence Length: 515 Download |
MAYLSYFFTL LMAPLLLGLF MFSTAVTGQL GLPYDVASKL HNDSQSINST ASDWGHIFHE 60 YAAAVLYPNS TNDIATLLQF ANNGSTTFGI AARGQGHSAR GQAMAKDGIV INMTTLNNMG 120 SRIVVSQSGE YADVGGEQLW IDVLRATVDQ GLSPVSWTDY LYLSVGGTLS NAGISGQTFR 180 YGPQITNVYE LDVVTGKGDV ITCSSKQTSE LFYSALGGLG QVGIITRARI ALQPAPNRAV 240 WIRLFYSDFS AFSKDQELLI ASKGKQGSVG FDYVEGFVLM PQGPVDLSFY SVADQPRITA 300 LLEQYGILYT IEIAKYYDDK AAKTIAKVVE ILLKQFSYIP GFIFQQDVSY IDFLNRVHTE 360 EKFLRTLGLW EVAHPWLNLF VPKSGIADFD SGVFKGILLK QKVPAGLVIV YPMNRNKWDD 420 KMTAVIPEED VFYVVALLHS SGLEEWQLFD EVNAQILQFC NDTGIEIKQY LPHYEKQQDW 480 TDHFGSKWQT FQEMKVKYDP NKILAPGQRV FDDL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 5.0e-7 | 52 | 245 | 202 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. | ||
pfam01565 | FAD_binding_4 | 1.0e-24 | 62 | 204 | 144 | + FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. | ||
COG0277 | GlcD | 1.0e-25 | 43 | 508 | 475 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam09265 | Cytokin-bind | 2.0e-133 | 236 | 511 | 284 | + Cytokinin dehydrogenase 1, FAD and cytokinin binding. Members of this family adopt an alpha+beta sandwich structure with an antiparallel beta-sheet, in a ferredoxin-like fold. They are predominantly found in plant cytokinin dehydrogenase 1, where they are capable of binding both FAD and cytokinin substrates. The substrate displays a 'plug-into-socket' binding mode that seals the catalytic site and precisely positions the carbon atom undergoing oxidation in close contact with the reactive locus of the flavin. | ||
PLN02441 | PLN02441 | 0 | 23 | 511 | 498 | + cytokinin dehydrogenase |
Gene Ontology | |
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GO Term | Description |
GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
GO:0009690 | cytokinin metabolic process |
GO:0016491 | oxidoreductase activity |
GO:0019139 | cytokinin dehydrogenase activity |
GO:0050660 | flavin adenine dinucleotide binding |
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 | 3s1e_A | 0 | 39 | 512 | 28 | 516 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
PDB | 3s1c_A | 0 | 39 | 512 | 28 | 516 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
PDB | 3dq0_A | 0 | 39 | 512 | 28 | 516 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
PDB | 3c0p_A | 0 | 39 | 512 | 28 | 516 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
PDB | 3bw7_A | 0 | 39 | 512 | 28 | 516 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |