| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s403_31V6.1 |
| Family | AA7 |
| Protein Properties | Length: 630 Molecular Weight: 70038 Isoelectric Point: 6.2959 |
| Chromosome | Chromosome/Scaffold: 403 Start: 153987 End: 158480 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 157 | 347 | 1.1e-24 |
| PGAVIYPKSVRDVQVAVRAVRSSRGFDLTLAAKGRGHSVHGQAQALNGVVMEMSSLKGIRVVPHGEPGYLQPFVDAAGGELWIDVLKATLREGLAPRSWT DYLYLSIGGTLSNAGVGGQTFLFGPEISNVLQLDVVTGTGQSVKCSPTQNADLFHGVLGGLGQFGIITSARIILEPAHEKVRWIRVMYTDF | |||
| Full Sequence |
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| Protein Sequence Length: 630 Download |
| MVTMVLLPKK SIPELIHVPD NRLLLTTLEP YNTTSLIELA GKEVHLAQIR RRKIVQRDSR 60 CEASQSNMIG ASILGSWTCI AWSIASWTLL VCLLLPRTRK GQYSDENAYI LTNYEDGSCL 120 SHEHRDLLSS LHLDGSLTFS NLSSAATDFG LVRFSLPGAV IYPKSVRDVQ VAVRAVRSSR 180 GFDLTLAAKG RGHSVHGQAQ ALNGVVMEMS SLKGIRVVPH GEPGYLQPFV DAAGGELWID 240 VLKATLREGL APRSWTDYLY LSIGGTLSNA GVGGQTFLFG PEISNVLQLD VVTGTGQSVK 300 CSPTQNADLF HGVLGGLGQF GIITSARIIL EPAHEKVRWI RVMYTDFAAF TRDQEMLVSQ 360 PPESAFDYIE GFVVLKTEDS INGWNSVPFD SKKIDPSVIP EEGGSVLYYI ELVKNFSSND 420 TDTVNETVER MLAPLSFIPA LVFTIDVSYE KFLNRLHDVE VNLDSHGLWD IPHPWLNLFV 480 PRSSIASFDA LIFKHLIKSD FNGPILIYPL KRDKWDSQSS AVIPDESVFY LVGFLRISLP 540 SSGPPLSSLI AENDKIMEVC HNASLGCKMY LPEYEDTESW KFHFGNRWET FSRRKHKYDP 600 EFILAPGQNI FPRIRAHDHP DNKLATTVV* 660 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01565 | FAD_binding_4 | 8.0e-17 | 182 | 302 | 122 | + 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-20 | 146 | 610 | 472 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam09265 | Cytokin-bind | 1.0e-117 | 336 | 611 | 280 | + 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 | 138 | 614 | 480 | + 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 |
| RefSeq | XP_001776926.1 | 0 | 101 | 613 | 2 | 515 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001777489.1 | 0 | 125 | 613 | 1 | 492 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001777510.1 | 0 | 73 | 627 | 6 | 561 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001784400.1 | 0 | 128 | 613 | 1 | 480 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001786014.1 | 0 | 137 | 613 | 2 | 482 | predicted protein [Physcomitrella patens subsp. patens] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2q4w_A | 0 | 130 | 613 | 33 | 522 | A Chain A, Structure Of The Complex Of A Mitotic Kinesin With Its Calcium Binding Regulator |
| PDB | 2exr_A | 0 | 130 | 613 | 33 | 522 | A Chain A, X-Ray Structure Of Cytokinin OxidaseDEHYDROGENASE (CKX) FROM Arabidopsis Thaliana At5g21482 |
| PDB | 3s1d_A | 0 | 128 | 611 | 20 | 515 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3s1c_A | 0 | 128 | 611 | 20 | 515 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| PDB | 3dq0_A | 0 | 128 | 611 | 20 | 515 | A Chain A, Glu381ser Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenosine |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FC349116 | 258 | 245 | 502 | 0 |
| HO781924 | 478 | 139 | 612 | 0 |
| FC355455 | 259 | 353 | 611 | 0 |
| ES837714 | 286 | 250 | 535 | 0 |
| ES791244 | 351 | 188 | 534 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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