| Basic Information | |
|---|---|
| Species | Oryza sativa |
| Cazyme ID | LOC_Os01g10110.1 |
| Family | AA7 |
| Protein Properties | Length: 566 Molecular Weight: 60021.2 Isoelectric Point: 6.5899 |
| Chromosome | Chromosome/Scaffold: 1 Start: 5270103 End: 5275678 |
| Description | cytokinin oxidase 3 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 78 | 271 | 3.4e-23 |
| AAAVLYPSRPADIAALLRASCARPAPFAVSARGCGHSVHGQASAPDGVVVDMASLGRLQGGGARRLAVSVEGRYVDAGGEQLWVDVLRASMAHGLTPVSW TDYLHLTVGGTLSNAGISGQAFRHGPQISNVLELDVITGVGEMVTCSKEKAPDLFDAVLGGLGQFGVITRARIPLAPAPARARWVRFVYTTAAA | |||
| Full Sequence |
|---|
| Protein Sequence Length: 566 Download |
| MKQEQVRMAV LLMLNCFVKA TAPPPWPPSA SSASFLDDLG DLGIAPLIRA DEAGTARASA 60 DFGNLSVAGV GAPRLAAAAA VLYPSRPADI AALLRASCAR PAPFAVSARG CGHSVHGQAS 120 APDGVVVDMA SLGRLQGGGA RRLAVSVEGR YVDAGGEQLW VDVLRASMAH GLTPVSWTDY 180 LHLTVGGTLS NAGISGQAFR HGPQISNVLE LDVITGVGEM VTCSKEKAPD LFDAVLGGLG 240 QFGVITRARI PLAPAPARAR WVRFVYTTAA AMTADQERLI AVDRAGGAGA VGGLMDYVEG 300 SVHLNQGLVE TWRTQPQPPS PSSSSSSSFF SDADEARVAA LAKEAGGVLY FLEGAIYFGG 360 AAGPSAADVD KRMDVLRREL RHERGFVFAQ DVAYAGFLDR VHDGELKLRA AGLWDVPHPW 420 LNLFLPRSGV LAFADGVFHG ILSRTPAMGP VLIYPMNRNK WDSNMSAVIT DDDGDEVFYT 480 VGILRSAAAA GDVGRLEEQN DEILGFCEVA GIAYKQYLPY YGSQAEWQKR HFGANLWPRF 540 VQRKSKYDPK AILSRGQGIF TSPLA* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01678 | FAD_lactone_ox | 2.0e-5 | 184 | 245 | 62 | + sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include 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. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. | ||
| COG0277 | GlcD | 3.0e-16 | 89 | 559 | 480 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 9.0e-19 | 89 | 224 | 137 | + 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. | ||
| pfam09265 | Cytokin-bind | 3.0e-135 | 264 | 560 | 301 | + 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 | 41 | 560 | 522 | + cytokinin dehydrogenase | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0003824 | catalytic activity |
| GO:0005773 | vacuole |
| GO:0008152 | metabolic process |
| GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
| GO:0009056 | catabolic process |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| DDBJ | BAB56095.1 | 0 | 8 | 565 | 1 | 558 | putative cytokinin oxidase [Oryza sativa Japonica Group] |
| DDBJ | BAE16612.1 | 0 | 1 | 565 | 1 | 565 | cytokinin oxidase/dehydrogenase [Oryza sativa Japonica Group] |
| GenBank | EEC70112.1 | 0 | 1 | 565 | 1 | 563 | hypothetical protein OsI_00771 [Oryza sativa Indica Group] |
| GenBank | EEE54051.1 | 0 | 1 | 565 | 1 | 525 | hypothetical protein OsJ_00744 [Oryza sativa Japonica Group] |
| RefSeq | XP_002455003.1 | 0 | 48 | 565 | 67 | 573 | hypothetical protein SORBIDRAFT_03g002810 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3s1d_A | 0 | 25 | 561 | 15 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3s1c_A | 0 | 25 | 561 | 15 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3dq0_A | 0 | 25 | 561 | 15 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3c0p_A | 0 | 25 | 561 | 15 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3bw7_A | 0 | 25 | 561 | 15 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| cytokinins degradation | RXN-4621 | EC-1.5.99 | isopentenyladenine:FAD oxidoreductase |
| cytokinins degradation | RXN-4661 | EC-1.5.99 | trans-zeatin:FAD oxidoreductase |
