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Basic Information | |
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Species | Arabidopsis lyrata |
Cazyme ID | 867825 |
Family | AA7 |
Protein Properties | Length: 529 Molecular Weight: 59356 Isoelectric Point: 8.6219 |
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 | 62 | 255 | 4.5e-24 |
NRYQLIPLAVLHPKSVSDIASAIRHIWMMGPHSQLTVAARGRGHSLQGQAQTRHGVVIHMESLHPQKLQVYSVDAPAPYVDVSGGELWINILHETLKYGL APKSWTDYLHLTVGGTLSNAGISGQAFRHGPQISNVHQLEIVTGKGEILNCSKRQNSDLFDGVLGGLGQFGIITRARIALEPAPTMVKWIRVLY |
Full Sequence |
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Protein Sequence Length: 529 Download |
MSYLLRKRTM LIVRSFTILL LSCIAFKLAC CFSSSISSLK ALPLVGHLEF EDVHHASRDF 60 GNRYQLIPLA VLHPKSVSDI ASAIRHIWMM GPHSQLTVAA RGRGHSLQGQ AQTRHGVVIH 120 MESLHPQKLQ VYSVDAPAPY VDVSGGELWI NILHETLKYG LAPKSWTDYL HLTVGGTLSN 180 AGISGQAFRH GPQISNVHQL EIVTGKGEIL NCSKRQNSDL FDGVLGGLGQ FGIITRARIA 240 LEPAPTMVKW IRVLYLDFSA FAKDQEQLIS ADNKFDYIEG FVIINRTGLL NNWRLSFTPE 300 EPLEASQFKS DGRTLYCLEL AKYLKQDNKD VINQEVKETL SELSYVSSTL FSTEVTYEAF 360 LDRVHVSEVK LRSKGQWEVP HPWLNLLVPR STIKEFAKGV FGNILTDTSN GPVIVYPVNK 420 SKWDNQTSAV TPEEEVFYLV AILTSAVPGK EDGGGVEQIL KRNRRILEFS EEAGIGLKQY 480 LPHYTTREEW RSHFGAKWGE FVRRKSRYDP LAILAPGQRI FEKAVSYS* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 3.0e-9 | 68 | 302 | 235 | + 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 | 2.0e-23 | 68 | 213 | 147 | + 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 | 5.0e-25 | 61 | 518 | 465 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam09265 | Cytokin-bind | 6.0e-149 | 245 | 521 | 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 | 6 | 528 | 530 | + 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 |
DDBJ | BAF00384.1 | 0 | 10 | 528 | 1 | 520 | cytokinin oxidase -like protein [Arabidopsis thaliana] |
RefSeq | NP_191903.3 | 0 | 1 | 528 | 1 | 533 | CKX6 (CYTOKININ OXIDASE/DEHYDROGENASE 6); cytokinin dehydrogenase [Arabidopsis thaliana] |
Swiss-Prot | Q9LY71 | 0 | 10 | 528 | 1 | 504 | CKX6_ARATH RecName: Full=Cytokinin dehydrogenase 6; AltName: Full=Cytokinin oxidase 6; Short=CKO6; Short=AtCKX6; Short=AtCKX7; Flags: Precursor |
RefSeq | XP_002304773.1 | 0 | 10 | 528 | 1 | 517 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002332424.1 | 0 | 4 | 528 | 8 | 530 | cytokinin oxidase [Populus trichocarpa] |
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 | 3s1d_A | 0 | 37 | 522 | 18 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3s1c_A | 0 | 37 | 522 | 18 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3dq0_A | 0 | 37 | 522 | 18 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3c0p_A | 0 | 37 | 522 | 18 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
PDB | 3bw7_A | 0 | 37 | 522 | 18 | 516 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
ES837714 | 288 | 161 | 448 | 0 |
DV137371 | 268 | 202 | 469 | 0 |
DY963441 | 302 | 46 | 346 | 0 |
JK618028 | 277 | 65 | 341 | 0 |
HO781924 | 495 | 33 | 521 | 0 |
Sequence Alignments (This image is cropped. Click for full image.) |
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