Sulfur Containing Compound Database
Gene name | CYP81F2 |
AGI ID | AT5G57220 |
Gene length | 491 |
Uniprot ID | Q9LVD6 |
Protein Name | Cytochrome P450 81F2 |
Synonym | IGM1 |
EC number | EC 1.14.-.- |
Entrez Gene | 835828 |
Refseq mrna | NM_125104 |
Refseq protein | NP_200532 |
Function | All four Arabidopsis CYP81F gene products had the capacity to modify the indole GSL structure. CYP81F1; CYP81F2; and CYP81F3 but not CYP81F4 catalyzed the conversion of indol-3-yl-methyl GSL (I3M) to 4-hydroxy-indol-3-yl-methyl (4OH-I3M) and all four CYP81Fs converted I3M to 1-hydroxy-indol-3-yl-methyl GSL (1OH-I3M) (Pfalz et al. 2011) |
Group | GSL core structure synthesis |
Reference | Bednarek et al. (2009); Hiruma et al. (2010); Pfalz et al. (2009) |
Organism | AGI ID | Gene Name | Protein Name | Identity | E-Value | Description |
---|---|---|---|---|---|---|
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
91 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
89 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
88 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
88 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
88 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
74 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
74 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
73 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
72 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
69 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
69 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
69 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
63 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
63 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
63 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
65 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
56 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
55 |
0.00E+00 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
54 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
54 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
54 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
54 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
56 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
54 |
0.00E+00 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
57 |
0.00E+00 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
4.00E-180 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
57 |
4.00E-180 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
4.00E-179 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
4.00E-178 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
52 |
8.00E-177 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
52 |
1.00E-176 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
52 |
2.00E-176 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
2.00E-175 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
5.00E-173 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
53 |
2.00E-169 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
52 |
6.00E-167 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
52 |
3.00E-166 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
51 |
1.00E-165 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
52 |
5.00E-164 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
48 |
5.00E-162 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
52 |
6.00E-161 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
49 |
7.00E-161 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
49 |
1.00E-156 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
49 |
2.00E-155 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
50 |
4.00E-154 |
||
Cabbage |
CYP81F2 |
Cytochrome P450 81F2 |
50 |
4.00E-150 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
44 |
7.00E-143 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
45 |
1.00E-141 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
44 |
9.00E-139 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
43 |
2.00E-137 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
42 |
2.00E-128 |
||
Broccoli |
CYP81F2 |
Cytochrome P450 81F2 |
42 |
2.00E-127 |
||
Papaya |
CYP81F2 |
Cytochrome P450 81F2 |
40 |
2.00E-111 |
GO ID | Ontology | GO Term | Description |
---|---|---|---|
BP |
defense response to insect |
A response to protect an organism from a directly detected or perceived external threat from an insect or insects to that organism. |
|
MF |
iron ion binding |
Interacting selectively and non-covalently with iron (Fe) ions. |
|
BP |
response to bacterium |
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a bacterium. |
|
BP |
induced systemic resistance |
A response to non-pathogenic bacteria that confers broad spectrum systemic resistance to disease that does not depend upon salicylic acid signaling. |
|
BP |
indole glucosinolate biosynthetic process |
The chemical reactions and pathways resulting in the formation of indole glucosinolates, sulfur-containing compounds that have a common structure linked to an R group derived from tryptophan. |
|
CC |
membrane |
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
|
CC |
integral component of membrane |
The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
|
MF |
oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen |
Catalysis of an oxidation-reduction (redox) reaction in which hydrogen or electrons are transferred from NADH or NADPH and one other donor, and one atom of oxygen is incorporated into one donor. |
|
BP |
glucosinolate metabolic process |
The chemical reactions and pathways involving glucosinolates, substituted thioglucosides found in rapeseed products and related cruciferae. They are metabolized to a variety of toxic products which are most likely the cause of hepatocytic necrosis in anim |
|
MF |
oxygen binding |
Interacting selectively and non-covalently with oxygen (O2). |
|
MF |
heme binding |
Interacting selectively and non-covalently with heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring. |
|
BP |
indole glucosinolate metabolic process |
The chemical reactions and pathways resulting in the formation of indole glucosinolates. Glucosinolates are sulfur-containing compounds that have a common structure linked to an R group derived from tryptophan; indoles are biologically active substances b |
|
BP |
defense response to bacterium |
Reactions triggered in response to the presence of a bacterium that act to protect the cell or organism. |
|
BP |
defense response to fungus |
Reactions triggered in response to the presence of a fungus that act to protect the cell or organism. |
|
BP |
defense response by callose deposition in cell wall |
Any process in which callose is transported to, and/or maintained in, the cell wall during the defense response. Callose is a linear 1,3-beta-d-glucan formed from UDP-glucose and is found in certain plant cell walls. |
|
BP |
oxidation-reduction process |
A metabolic process that results in the removal or addition of one or more electrons to or from a substance, with or without the concomitant removal or addition of a proton or protons. |
|
BP |
cellular response to hypoxia |
Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below n |
Pubmed ID | Authors | Year | Title | Journal | Description |
---|---|---|---|---|---|
Bednarek, P., Pislewska-Bednarek, M., Svatos, A., Schneider, B., Doubsky, J., Mansurova, M., Humphry, M., Consonni, C., Panstruga, R., Sanchez-Vallet, A., Molina, A. & Schulze-Lefert, P. |
2009 |
A Glucosinolate Metabolism Pathway in Living Plant Cells Mediates Broad-Spectrum Antifungal Defense |
Science |
||
Hiruma, K., Onozawa-Komori, M., Takahashi, F., Asakura, M., Bednarek, P., Okuno, T., Schulze-Lefert, P. & Takano, Y. |
2010 |
Entry mode-dependent function of an indole glucosinolate pathway in Arabidopsis for nonhost resistance against anthracnose pathogens |
Plant Cell |
||
Pfalz, M., Vogel, H. & Kroymann, J. |
2009 |
The Gene Controlling the Indole Glucosinolate Modifier1 Quantitative Trait Locus Alters Indole Glucosinolate Structures and Aphid Resistance in Arabidopsis |
Plant Cell |