y
Basic Information | |
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Species | Populus trichocarpa |
Cazyme ID | Potri.016G044100.1 |
Family | AA7 |
Protein Properties | Length: 541 Molecular Weight: 60634 Isoelectric Point: 7.2682 |
Chromosome | Chromosome/Scaffold: 16 Start: 2750878 End: 2753123 |
Description | cytokinin oxidase/dehydrogenase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 80 | 274 | 5.6e-24 |
NRYHFLPLAVLHPNSVSDISNTIKHIFKMGSTSKLTVAARGHSHSLQGQAQAHQGIVINMESLQGPEMQIHTGELPYVDASGGDLWINILHETLKYGLAP KSWTDYLHLTVGGTLSNAGISGQAFKHGPQINNIYQLEVVTGKGEVVTCTEKQNAELFYSVLGGLGQFGIITRARISLEPAPKMVKWIRVLYDEF |
Full Sequence |
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Protein Sequence Length: 541 Download |
MGSPPSASLK QNNLIFLVFI MILFFCSIPD KANLCSNQSS VNPSGVPYKS SSNISSLETL 60 QLDGYFSFDH IDYAAKDFGN RYHFLPLAVL HPNSVSDISN TIKHIFKMGS TSKLTVAARG 120 HSHSLQGQAQ AHQGIVINME SLQGPEMQIH TGELPYVDAS GGDLWINILH ETLKYGLAPK 180 SWTDYLHLTV GGTLSNAGIS GQAFKHGPQI NNIYQLEVVT GKGEVVTCTE KQNAELFYSV 240 LGGLGQFGII TRARISLEPA PKMVKWIRVL YDEFSKFSND QERLISSKDS FDYIEGLVII 300 NRTGLLNNWR SSFNPKDPLQ ASRFTSEGKT LYCLEIAKYF SPDESDIMNQ KTESLLSELS 360 YISSTLFLSE VSYVEFLDRV HLSEIKLRSK GLWEIPHPWM NLLIPRTNII EFAQEVFGNI 420 LTGNSNGPIL IYPVNKSKWN NRTSLITPDE ETFYQVAFLS SAMPSSTGRD GLFHILAQNQ 480 RILDFCSKAG LGAKQYMPHY STQEEWQAHF GPQWEVFVKR KSTYDPLAIL APGQRIFRRK 540 * 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01565 | FAD_binding_4 | 4.0e-19 | 86 | 229 | 145 | + 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 | 2.0e-19 | 63 | 337 | 282 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam09265 | Cytokin-bind | 3.0e-135 | 261 | 537 | 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 | 10 | 539 | 539 | + 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 - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI33379.1 | 0 | 1 | 539 | 1 | 539 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284560.1 | 0 | 21 | 539 | 1 | 519 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002308930.1 | 0 | 1 | 540 | 1 | 539 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002323274.1 | 0 | 1 | 540 | 1 | 540 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002534458.1 | 0 | 1 | 540 | 1 | 540 | gulonolactone oxidase, putative [Ricinus communis] |
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 | 2q4w_A | 0 | 49 | 539 | 25 | 522 | A Chain A, Crystal Structure Of Human Glcat-S Apo Form |
PDB | 2exr_A | 0 | 49 | 539 | 25 | 522 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
PDB | 3s1d_A | 0 | 55 | 537 | 18 | 515 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3s1c_A | 0 | 55 | 537 | 18 | 515 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3dq0_A | 0 | 55 | 537 | 18 | 515 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cytokinins degradation | RXN-4621 | EC-1.5.99 | isopentenyladenine:FAD oxidoreductase |