Sulfur Containing Compound Database
Gene name | APR3 |
AGI ID | AT4G21990 |
Gene length | 458 |
Uniprot ID | P92980 |
Protein Name | 5'-adenylylsulfate reductase 3 chloroplastic |
Synonym | PRH26 |
EC number | EC 1.8.4.9 |
Entrez Gene | 828288 |
Refseq mrna | NM_118320 |
Refseq protein | NP_193930 |
Function | Using trans-activation assays two isoforms of APK; APK1 and APK2 are regulated by both classes of GSL MYB transcription factors; whereas two ATPS genes; ATPS1 and ATPS3 are differentially regulated by these two groups of MYB factors. The adenosine 5-phosphosulfate reductases APR1; APR2; and APR3 which participate in primary sulfate reduction are also activated by the MYB factors (Yatusevich et al. 2010) |
Group | GSL core structure synthesis |
Reference | Yatusevich et al. (2010) |
Organism | AGI ID | Gene Name | Protein Name | Identity | E-Value | Description |
---|---|---|---|---|---|---|
Broccoli |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
91 |
0.00E+00 |
||
Cabbage |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
89 |
0.00E+00 |
||
Cabbage |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
89 |
0.00E+00 |
||
Cabbage |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
88 |
0.00E+00 |
||
Broccoli |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
88 |
0.00E+00 |
||
Cabbage |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
82 |
0.00E+00 |
||
Broccoli |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
82 |
0.00E+00 |
||
Papaya |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
79 |
0.00E+00 |
||
Cabbage |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
76 |
0.00E+00 |
||
Papaya |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
76 |
0.00E+00 |
||
Papaya |
APR3 |
5'-adenylylsulfate reductase 3 chloroplastic |
73 |
0.00E+00 |
GO ID | Ontology | GO Term | Description |
---|---|---|---|
BP |
sulfate assimilation |
The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds. |
|
MF |
phosphoadenylyl-sulfate reductase (thioredoxin) activity |
Catalysis of the reaction: adenosine 3',5'-diphosphate + H(+) + sulfite + thioredoxin disulfide = 3'-phospho-5'-adenylyl sulfate + thioredoxin. Thioredoxin disulfide is the oxidized form of thioredoxin; 3'-phosphoadenosine 5'-phosphosulfate is also known |
|
CC |
chloroplast |
A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma. |
|
MF |
adenylyl-sulfate reductase activity |
Catalysis of the reaction: AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor. |
|
MF |
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor |
Catalysis of an oxidation-reduction (redox) reaction in which a sulfur-containing group acts as a hydrogen or electron donor and reduces disulfide. |
|
BP |
cysteine biosynthetic process |
The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid. |
|
BP |
sulfate reduction |
The chemical reactions and pathways resulting in the reduction of sulfate to another sulfur-containing ion or compound such as hydrogen sulfide, adenosine-phosphosulfate (APS) or thiosulfate. |
|
MF |
adenylyl-sulfate reductase (glutathione) activity |
Catalysis of the reaction: AMP + glutathione disulfide + H(+) + sulfite = 5'-adenylyl sulfate + 2 glutathione. |
|
BP |
cell redox homeostasis |
Any process that maintains the redox environment of a cell or compartment within a cell. |
|
MF |
metal ion binding |
Interacting selectively and non-covalently with any metal ion. |
|
MF |
4 iron, 4 sulfur cluster binding |
Interacting selectively and non-covalently with a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
|
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. |
Pubmed ID | Authors | Year | Title | Journal | Description |
---|---|---|---|---|---|
Yatusevich, R., Mugford, S.G., Matthewman, C., Gigolashvili, T., Frerigmann, H., Delaney, S., Koprivova, A. & Flu, U. |
2010 |
Genes of primary sulfate assimilation are part of the glucosinolate biosynthetic network in Arabidopsis thaliana |
Plant Journal |