Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.003G136500.1 |
Family | AA7 |
Protein Properties | Length: 577 Molecular Weight: 64008 Isoelectric Point: 5.0218 |
Chromosome | Chromosome/Scaffold: 03 Start: 32819603 End: 32824801 |
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 | 60 | 252 | 1.6e-25 |
VHDNPFAIFSPSSISDISLLINFSNSLPIPFTIAPRGQAHSVNGQAMTNDGVVVNMTELNGFRNGSGIVVVSDGTPYADVGGEQIWIDVLHATLEHGLTP LSWTDYLFLSVAGTLSNAGISGQSFRFGPQISNVHQLDVVTGKGDLVTCSSENNSELFYAVLGGLGQFGIITRARIALGPAPTRVKWLRLLYN |
Full Sequence |
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Protein Sequence Length: 577 Download |
MASYFRFSKA LVMLGLTFVV LTQAQSQPWS LLQAPKDLTL KLIRDPVTLS LASTDFGHIV 60 HDNPFAIFSP SSISDISLLI NFSNSLPIPF TIAPRGQAHS VNGQAMTNDG VVVNMTELNG 120 FRNGSGIVVV SDGTPYADVG GEQIWIDVLH ATLEHGLTPL SWTDYLFLSV AGTLSNAGIS 180 GQSFRFGPQI SNVHQLDVVT GKGDLVTCSS ENNSELFYAV LGGLGQFGII TRARIALGPA 240 PTRVKWLRLL YNNFSAFSAD QEHLISLNGR NETIAADYVE GFLLLNQPPL DLSSFPAPDQ 300 PRISSLVTQY GIIYIIELVK YYDNSTQEHI EEEVELLVEG LKFVPTFMFE KDVSYEEFLN 360 RVHSDELFLR SQGLWDVPHP WINLFVPGSR ISDFNEGVFK GIILKQNITA GIAIIYPMNR 420 SKWNDKMSAV TPNEDVFYAV SLLHATGFDK VEEFQAQNQQ ILDFCEDAVN GIPTKEFTPK 480 KGLRQGDPLT PFFFLKASKG LLGVSRNVVD KSLFESIEVG YKKVTVHMLQ YADDTLFFCA 540 ANIKSVHNLR VMLNCFELAF GLKVDFFEER NWRGGG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01678 | FAD_lactone_ox | 2.0e-7 | 96 | 240 | 149 | + 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. | ||
COG0277 | GlcD | 2.0e-17 | 92 | 241 | 156 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 1.0e-20 | 92 | 209 | 119 | + 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 | 3.0e-93 | 241 | 479 | 247 | + 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 | 1 | 479 | 486 | + cytokinin dehydrogenase |
Gene Ontology | |
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GO Term | Description |
GO:0003723 | RNA binding |
GO:0003964 | RNA-directed DNA polymerase activity |
GO:0006278 | RNA-dependent DNA replication |
GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
GO:0009690 | cytokinin metabolic process |
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 | ABN05767.1 | 0 | 41 | 477 | 1 | 454 | FAD linked oxidase, N-terminal [Medicago truncatula] |
GenBank | ABN08744.1 | 0 | 35 | 477 | 34 | 493 | FAD linked oxidase, N-terminal [Medicago truncatula] |
GenBank | ACM79256.1 | 0 | 37 | 485 | 41 | 490 | cytokinin oxidase/dehydrogenase [Gossypium hirsutum] |
RefSeq | XP_002308300.1 | 0 | 11 | 479 | 12 | 487 | cytokinin oxidase [Populus trichocarpa] |
RefSeq | XP_002514119.1 | 0 | 37 | 479 | 42 | 489 | 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 | 20 | 480 | 7 | 476 | A Chain A, Clostridium Beijerinckii Flavodoxin Mutant: N137a Oxidized (150k) |
PDB | 2qpm_A | 0 | 20 | 480 | 7 | 476 | A Chain A, Leu492ala Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With Benzylurea Inhibitor Cpbu |
PDB | 3s1e_A | 0 | 20 | 480 | 7 | 476 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
PDB | 3s1c_A | 0 | 20 | 480 | 7 | 476 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |
PDB | 3dq0_A | 0 | 20 | 480 | 7 | 476 | A Chain A, Pro427gln Mutant Of Maize Cytokinin OxidaseDEHYDROGENASE COMPLEXED With N6-Isopentenyladenine |