Sulfur Containing Compound Database
Gene name | APR1 |
AGI ID | AT4G04610 |
Gene length | 465 |
Uniprot ID | P92979 |
Protein Name | 5'-adenylylsulfate reductase 1 chloroplastic |
Synonym | PRH19 |
EC number | EC 1.8.4.9 |
Entrez Gene | 825793 |
Refseq mrna | NM_116699 |
Refseq protein | NP_192370 |
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 |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
86 |
0.00E+00 |
||
Cabbage |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
85 |
0.00E+00 |
||
Cabbage |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
84 |
0.00E+00 |
||
Broccoli |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
84 |
0.00E+00 |
||
Broccoli |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
84 |
0.00E+00 |
||
Cabbage |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
84 |
0.00E+00 |
||
Papaya |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
81 |
0.00E+00 |
||
Cabbage |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
75 |
0.00E+00 |
||
Papaya |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
71 |
0.00E+00 |
||
Papaya |
APR1 |
5'-adenylylsulfate reductase 1 chloroplastic |
68 |
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. |
|
CC |
plastid |
Any member of a family of organelles found in the cytoplasm of plants and some protists, which are membrane-bounded and contain DNA. Plant plastids develop from a common type, the proplastid. |
|
CC |
chloroplast stroma |
The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis. |
|
MF |
adenylyl-sulfate reductase activity |
Catalysis of the reaction: AMP + sulfite + acceptor = adenylyl sulfate + reduced acceptor. |
|
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 |