| Basic Information | |
|---|---|
| Species | Setaria italica |
| Cazyme ID | Si013710m |
| Family | AA7 |
| Protein Properties | Length: 459 Molecular Weight: 47369.5 Isoelectric Point: 7.7814 |
| Chromosome | Chromosome/Scaffold: 6 Start: 29827236 End: 29830378 |
| Description | cytokinin oxidase 7 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 37 | 237 | 1.9e-32 |
| LVSAIPAAVVRPASADDVASAIRAAARTAGLTVAARGNGHSVAGQAMAEGGLVLDMRALALSRRPQMQLVGCPGGGNNGPCYADVPGGALWEEVLHWGVK NHGLAPASWTDYLRLTVGGTLSNGGVSGQSFRYGPQVSNVAELEVVTGDGDCRVCSPSSHPDLFFAVLGGLGQFGVITRARIPLRRAPRAVRWTRVVYAS F | |||
| Full Sequence |
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| Protein Sequence Length: 459 Download |
| MMLAYMDRAA AAAEPEDAGE PAPVAAGCAA ATDFGGLVSA IPAAVVRPAS ADDVASAIRA 60 AARTAGLTVA ARGNGHSVAG QAMAEGGLVL DMRALALSRR PQMQLVGCPG GGNNGPCYAD 120 VPGGALWEEV LHWGVKNHGL APASWTDYLR LTVGGTLSNG GVSGQSFRYG PQVSNVAELE 180 VVTGDGDCRV CSPSSHPDLF FAVLGGLGQF GVITRARIPL RRAPRAVRWT RVVYASFADY 240 TADAEWLVTR PPEEAFDYVE GFAFVNSDDP VNGWPSVPIP GGARFDASLL PAGAGPVLYC 300 LEVALYQYPD GAVEDDEDKV GPEHVGGAAG RRGLLPGGAA AVLPGRRAGG GRAGGAERRD 360 PPRVPRQRLR PQGLLPELPG RGGVGAPLRR RQVEALRGAQ GPLRPAGDPR AGPENLPQGP 420 GVRRRRVARA PAGGGGPGLA WHGRMGWGED QPGVSCWW* 480 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01678 | FAD_lactone_ox | 0.0002 | 131 | 213 | 83 | + 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 | 1.0e-11 | 75 | 214 | 146 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 4.0e-17 | 74 | 192 | 119 | + 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 | 4.0e-26 | 229 | 318 | 91 | + 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 | 1.0e-121 | 32 | 310 | 281 | + cytokinin dehydrogenase | ||
| Gene Ontology | |
|---|---|
| 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 - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | ADB81979.1 | 0 | 1 | 320 | 1 | 321 | cytokinin oxidase/dehydrogenase 3 [Triticum aestivum] |
| DDBJ | BAD09964.1 | 0 | 1 | 307 | 1 | 302 | putative cytokinin dehydrogenase [Oryza sativa Japonica Group] |
| RefSeq | NP_001146838.1 | 0 | 1 | 308 | 1 | 313 | cytokinin dehydrogenase 10 [Zea mays] |
| RefSeq | XP_002445610.1 | 0 | 30 | 308 | 17 | 302 | hypothetical protein SORBIDRAFT_07g022530 [Sorghum bicolor] |
| RefSeq | XP_002516133.1 | 0 | 2 | 310 | 1 | 320 | gulonolactone oxidase, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2q4w_A | 0 | 25 | 334 | 45 | 348 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 2exr_A | 0 | 25 | 334 | 45 | 348 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
| PDB | 3s1d_A | 0 | 26 | 266 | 35 | 276 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3kjm_A | 0 | 26 | 266 | 35 | 276 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 2qpm_A | 0 | 26 | 266 | 35 | 276 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FL714394 | 251 | 80 | 325 | 0 |
| CB673387 | 190 | 118 | 307 | 0 |
| EG384602 | 227 | 74 | 267 | 0 |
| HO781924 | 274 | 33 | 306 | 0 |
| GR446435 | 274 | 33 | 306 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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