| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01001461001 |
| Family | AA7 |
| Protein Properties | Length: 608 Molecular Weight: 68642.7 Isoelectric Point: 8.4444 |
| Chromosome | Chromosome/Scaffold: 13 Start: 21182229 End: 21185913 |
| Description | cytokinin oxidase/dehydrogenase 6 |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 95 | 293 | 2.5e-23 |
| GNRYQFLPQAVLHPKSVSDIAMTIKHVWQMGPGSELTVAARGHGHSLQGQAQAHQGIVINMESLQGTEMQVYTGNFPYVDVSGGELWINILHESLKYGLA PKSWTDYLHLTVGGTLSNAGISGQAFRHGPQISNVHWLEVVTGKGEVINCSKNQNGDLFHSVLGGLGQFGIITRARISLEPAPKMVKWIRVLYSDFSTF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 608 Download |
| MAAREWSVSR AKEAMGGFCL WLLPSFLKKK MRYPAISFLR PSSIRFIASF VILFLGCLTA 60 NISLCLPIIP SSLETLSVDG HFSFHGIEHA ARDFGNRYQF LPQAVLHPKS VSDIAMTIKH 120 VWQMGPGSEL TVAARGHGHS LQGQAQAHQG IVINMESLQG TEMQVYTGNF PYVDVSGGEL 180 WINILHESLK YGLAPKSWTD YLHLTVGGTL SNAGISGQAF RHGPQISNVH WLEVVTGKGE 240 VINCSKNQNG DLFHSVLGGL GQFGIITRAR ISLEPAPKMV KWIRVLYSDF STFARDQEYL 300 ISAENTFDYI EGFVIINRTG LLNNWRSSFN PQDPVQASQF ESDGKILFCL ELTKNFKVDN 360 TNINQEVESL LSQLSYIPST LFLSEVPYID FLDRVHVSEV KLHSKGLWEV PHPWLNLLVP 420 KSKIHNFAEE VFGKILKDTS NGPILIYPVN KSKWDNRTSA VIPEEDIFYL VAFLSSAVPS 480 STGTDGLEYI LSRNKRILDF CKTARLGVKQ YLPHYTTQEE WRTHFGPRWE AFAQRKSAYD 540 PLAILAPGHR IFRKATPFFP INDVYIKLMN KKQISFSHES KFQIHYCLQH QEVTHASEKY 600 EVAFIKP* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01679 | bact_FAD_ox | 1.0e-6 | 102 | 271 | 177 | + 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 | 7.0e-22 | 102 | 245 | 146 | + 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-23 | 95 | 553 | 469 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam09265 | Cytokin-bind | 6.0e-153 | 277 | 552 | 281 | + 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 | 40 | 558 | 529 | + 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 |
| EMBL | CBI28611.1 | 0 | 1 | 607 | 1 | 607 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002270841.1 | 0 | 31 | 559 | 1 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002304773.1 | 0 | 46 | 558 | 3 | 516 | cytokinin oxidase [Populus trichocarpa] |
| RefSeq | XP_002332424.1 | 0 | 31 | 558 | 1 | 529 | cytokinin oxidase [Populus trichocarpa] |
| RefSeq | XP_002513118.1 | 0 | 31 | 558 | 1 | 529 | Cytokinin dehydrogenase, 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 | 74 | 555 | 32 | 523 | A Chain A, Lip5(mit)2 |
| PDB | 2exr_A | 0 | 74 | 555 | 32 | 523 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
| PDB | 3s1d_A | 0 | 70 | 552 | 17 | 515 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3s1c_A | 0 | 70 | 552 | 17 | 515 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3dq0_A | 0 | 70 | 552 | 17 | 515 | 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 |
