y
Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00035115m |
Family | AA7 |
Protein Properties | Length: 523 Molecular Weight: 56282.1 Isoelectric Point: 6.526 |
Chromosome | Chromosome/Scaffold: 096394 Start: 183 End: 2396 |
Description | cytokinin oxidase 4 |
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 | 59 | 255 | 3.2e-22 |
TSAFPAAVLYPSSPADLGALLGAAYATPGWPYTIAFRGRGHSIMGQAFAPGGVVVDMASLGAAAAPRINVSADGRYVDAGGEQLWIDVLRASLARGVAPR SWTDYLYLTIGGTLSNAGVSGQTFRHGPQISNVFELDVITGRGETVTCSKELNADLFDAVLGGLGQFGVITRARIAVEPAPARARWVRLVYTDFATF |
Full Sequence |
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Protein Sequence Length: 523 Download |
MAVVCLLLAA LIASCHAQAT AGDRRPPWPA SLAALAAEGK LRTDSNATVP ASMDFGNITS 60 AFPAAVLYPS SPADLGALLG AAYATPGWPY TIAFRGRGHS IMGQAFAPGG VVVDMASLGA 120 AAAPRINVSA DGRYVDAGGE QLWIDVLRAS LARGVAPRSW TDYLYLTIGG TLSNAGVSGQ 180 TFRHGPQISN VFELDVITGR GETVTCSKEL NADLFDAVLG GLGQFGVITR ARIAVEPAPA 240 RARWVRLVYT DFATFTADQE RLVRPLPGGA FGPMSYVEGS VFVNQSLASD LKNTGFFSDA 300 DAARVVALAK ERNATAVYSI EATLNYDNAT AAASVDQVLK SVLDGLRFEP GFAFVRDVAY 360 VEFLDRVHNE EVALDKMGLW RVPHPWLNMF VPGSRIADFD RGVFKGILQG TDIVGPLIVY 420 PVNKAKWDDG MSAATPAEDV FYVVSLLFSS VANDLAKLQA QNQRILRFCD LAGIQYKSYL 480 ARYSDRGDWV RHFGTDKWSR FVEMKNKYDP KKLLSPGQDI FN* 540 |
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 | 167 | 238 | 72 | + 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 | 3.0e-18 | 63 | 207 | 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 | 6.0e-20 | 63 | 518 | 462 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam09265 | Cytokin-bind | 1.0e-132 | 239 | 521 | 287 | + 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 | 38 | 522 | 489 | + 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 |
PDB | 1W1O | 0 | 1 | 522 | 1 | 534 | A Chain A, Native Cytokinin Dehydrogenase |
PDB | 2QKN | 0 | 19 | 522 | 7 | 516 | A Chain A, Crystal Structure Of Maize Cytokinin OxidaseDEHYDROGENASE Complexed With Phenylurea Inhibitor Cppu |
RefSeq | NP_001105591.1 | 0 | 1 | 522 | 1 | 534 | cytokinin oxidase1 precursor [Zea mays] |
Swiss-Prot | Q9T0N8 | 0 | 1 | 522 | 1 | 534 | CKX1_MAIZE RecName: Full=Cytokinin dehydrogenase 1; AltName: Full=Cytokinin oxidase 1; Short=CKO 1; Short=COX 1; AltName: Full=ZmCKX1; Flags: Precursor |
RefSeq | XP_002455033.1 | 0 | 1 | 522 | 1 | 529 | hypothetical protein SORBIDRAFT_03g003280 [Sorghum bicolor] |
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 | 1w1s_A | 0 | 1 | 522 | 1 | 534 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1w1r_A | 0 | 1 | 522 | 1 | 534 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1w1q_A | 0 | 1 | 522 | 1 | 534 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 1w1o_A | 0 | 1 | 522 | 1 | 534 | A Chain A, Native Cytokinin Dehydrogenase |
PDB | 3s1c_A | 0 | 19 | 522 | 7 | 516 | A Chain A, Native Cytokinin Dehydrogenase |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cytokinins degradation | RXN-4621 | EC-1.5.99 | isopentenyladenine:FAD oxidoreductase |
cytokinins degradation | RXN-4641 | EC-1.5.99 | isopentenyl adenosine:FAD oxidoreductase |
cytokinins degradation | RXN-4661 | EC-1.5.99 | trans-zeatin:FAD oxidoreductase |
cytokinins degradation | RXN-4662 | EC-1.5.99 | cis-zeatin:FAD oxidoreductase |
cytokinins degradation | RXN-4681 | EC-1.5.99 | trans-zeatin riboside:FAD oxidoreductase |