Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.H03393.1 |
Family | AA7 |
Protein Properties | Length: 474 Molecular Weight: 53368 Isoelectric Point: 5.585 |
Chromosome | Chromosome/Scaffold: 8 Start: 49636014 End: 49639219 |
Description | cytokinin oxidase 3 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 62 | 254 | 1.1e-25 |
LIVRKIPAVVLRPSHPEDIAVLVAFANSKSSIPFTISARGCGHSVRGQAMARDGVVVDMTSLGNKTAVSWSQSLGHYADVGGQQLWINVLEETLKHGVTP VSWTDYLYLTVGGTLSNAGISGETFRYGPQISNVYEMDVITGTGHFFTCSPHKNPELFYSVLGGLGQFGIITRARIALGQAPNRAIWVRMLYS |
Full Sequence |
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Protein Sequence Length: 474 Download |
MAQNHPVVSH CMAITLILMS TLVCQSKLLN DPLYRELLSL PIASDLHIDP ESIAEASVDF 60 GLIVRKIPAV VLRPSHPEDI AVLVAFANSK SSIPFTISAR GCGHSVRGQA MARDGVVVDM 120 TSLGNKTAVS WSQSLGHYAD VGGQQLWINV LEETLKHGVT PVSWTDYLYL TVGGTLSNAG 180 ISGETFRYGP QISNVYEMDV ITGTGHFFTC SPHKNPELFY SVLGGLGQFG IITRARIALG 240 QAPNRAIWVR MLYSDFSAFT TDQERLISLH GRDQDEALDY VEGQLFMRRN SDSWISFFSL 300 SDRPRLMSLL TEHELLYCIE VAKFYDERTR STVDKDLKTI LKDLSHVPEF LFQKDVGYVD 360 FLNRVRAEEL TLRELGLWNV PHPWLNLFVP KSRIADFNTG VFKNIVLRKN ITTGPVLIYP 420 MNNDKWDDRM SAVIPDEDVF YTVGFLLSSG FKDWQEFDLQ NKEVLLFCED NGIK 480 |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
TIGR01679 | bact_FAD_ox | 0.0006 | 68 | 311 | 275 | + 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. |
COG0277 | GlcD | 9.0e-19 | 49 | 397 | 359 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
pfam01565 | FAD_binding_4 | 1.0e-24 | 68 | 211 | 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. |
pfam09265 | Cytokin-bind | 1.0e-107 | 243 | 474 | 239 | + 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 | 14 | 474 | 469 | + 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 |
GenBank | ACM79256.1 | 0 | 15 | 473 | 12 | 477 | cytokinin oxidase/dehydrogenase [Gossypium hirsutum] |
RefSeq | XP_002263754.1 | 0 | 1 | 474 | 1 | 474 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002264539.1 | 0 | 1 | 474 | 1 | 474 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002308300.1 | 0 | 1 | 474 | 1 | 481 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002514119.1 | 0 | 1 | 474 | 1 | 483 | 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 | 3kjm_A | 0 | 32 | 474 | 15 | 469 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 2qpm_A | 0 | 32 | 474 | 15 | 469 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
PDB | 1w1s_A | 0 | 7 | 474 | 3 | 487 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
PDB | 1w1r_A | 0 | 7 | 474 | 3 | 487 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
PDB | 1w1q_A | 0 | 7 | 474 | 3 | 487 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |