| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G303707_T01 |
| Family | AA7 |
| Protein Properties | Length: 569 Molecular Weight: 62146.2 Isoelectric Point: 6.7445 |
| Chromosome | Chromosome/Scaffold: 9 Start: 80487684 End: 80489879 |
| Description | cytokinin oxidase 3 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 77 | 275 | 1.3e-28 |
| VRAIPSGVFHPTSPSDIAALIRLSLSQPKPFAVAPRGRGHSARGQALAVGGVVVDMRSLHDHDHDHRAGHGRYRMNNAVPGAWVDVGGEQLWIDVLHATL EHDLAPRVWTDYLHITVGGTLSNGGIGGQAFRHGPQISNVHELDVVTGTGEMVSCSPGKNSDLFYAALGGLGQFGVITRARIALEPAPRRVLWVRLAYS | |||
| Full Sequence |
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| Protein Sequence Length: 569 Download |
| MQLADSSHLV APVPTLCSNM TARAAYLASF LIVTSFLPTS SSHSHVPAVT DALDIVSKIS 60 TEHDATIKAS MDFGHIVRAI PSGVFHPTSP SDIAALIRLS LSQPKPFAVA PRGRGHSARG 120 QALAVGGVVV DMRSLHDHDH DHRAGHGRYR MNNAVPGAWV DVGGEQLWID VLHATLEHDL 180 APRVWTDYLH ITVGGTLSNG GIGGQAFRHG PQISNVHELD VVTGTGEMVS CSPGKNSDLF 240 YAALGGLGQF GVITRARIAL EPAPRRVLWV RLAYSDVRSF TSDQELLISK RPAGGCGSGF 300 DYVEGQVQLN RTLTEGRRSS SFFSAPELDQ LARLAVATGS AAIYYIEGAM YYDDDTTTAS 360 SVNQKLETLL EELSFVPGLA FVRDVSYVDF LDRVGRDEQK LRSAGVWDVP HPWLNIFVPR 420 SRILDFDAGV FKGILKGTRP VGLILMYPMN KDRWDDRMTT ATPDEDVFYA VGLLRSAVAA 480 ADLEQLEREN AAVLEFCHRE GIGYRQYLPS HASLDGWRRH FGEKWSRFAA LKRKYDPRAI 540 LTPGQGIFFS AGHDLTDQQT GSDSRNVL* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01678 | FAD_lactone_ox | 1.0e-6 | 79 | 263 | 192 | + 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. | ||
| pfam01565 | FAD_binding_4 | 2.0e-22 | 81 | 232 | 153 | + 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-26 | 74 | 547 | 484 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam09265 | Cytokin-bind | 1.0e-148 | 264 | 548 | 288 | + 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 | 22 | 548 | 534 | + 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 |
| DDBJ | BAD17197.1 | 0 | 20 | 550 | 1 | 515 | putative cytokinin dehydrogenase 1 precursor [Oryza sativa Japonica Group] |
| DDBJ | BAD61835.1 | 0 | 25 | 547 | 5 | 529 | putative cytokinin oxidase [Oryza sativa Japonica Group] |
| GenBank | EAY85042.1 | 0 | 20 | 550 | 1 | 515 | hypothetical protein OsI_06399 [Oryza sativa Indica Group] |
| GenBank | EEC80843.1 | 0 | 56 | 547 | 1 | 487 | hypothetical protein OsI_23446 [Oryza sativa Indica Group] |
| RefSeq | XP_002438603.1 | 0 | 25 | 564 | 5 | 547 | hypothetical protein SORBIDRAFT_10g022590 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3s1e_A | 0 | 47 | 548 | 17 | 515 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
| PDB | 3s1c_A | 0 | 47 | 548 | 17 | 515 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
| PDB | 3dq0_A | 0 | 47 | 548 | 17 | 515 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
| PDB | 3c0p_A | 0 | 47 | 548 | 17 | 515 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
| PDB | 3bw7_A | 0 | 47 | 548 | 17 | 515 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
| Hydropathy |
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