Q74ZF6
Gene name |
MET3 |
Protein name |
Sulfate adenylyltransferase |
Names |
ATP-sulfurylase, Sulfate adenylate transferase, SAT |
Species |
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) |
KEGG Pathway |
ago:AGOS_AGR322W |
EC number |
2.7.7.4: Nucleotidyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q74ZF6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q74ZF6-F1 | Predicted | AlphaFoldDB |
No variants for Q74ZF6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q74ZF6 | |||||
No associated diseases with Q74ZF6
11 regional properties for Q74ZF6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 1079 - 1346 | IPR000719 |
| domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 1080 - 1337 | IPR001245 |
| domain | Sema domain | 27 - 516 | IPR001627 |
| domain | IPT domain | 563 - 656 | IPR002909-1 |
| domain | IPT domain | 657 - 740 | IPR002909-2 |
| domain | IPT domain | 742 - 837 | IPR002909-3 |
| domain | IPT domain | 839 - 935 | IPR002909-4 |
| active_site | Tyrosine-protein kinase, active site | 1201 - 1213 | IPR008266 |
| domain | PSI domain | 520 - 563 | IPR016201 |
| binding_site | Protein kinase, ATP binding site | 1085 - 1111 | IPR017441 |
| domain | Tyrosine-protein kinase, catalytic domain | 1079 - 1338 | IPR020635 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.7.4 | Nucleotidyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| sulfate adenylyltransferase (ATP) activity | Catalysis of the reaction: ATP + sulfate = diphosphate + adenylylsulfate. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cysteine biosynthetic process | The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid. |
| hydrogen sulfide biosynthetic process | The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S. |
| methionine biosynthetic process | The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins. |
| sulfate assimilation via adenylyl sulfate reduction | The pathway by which inorganic sulfate is activated, reduced and incorporated into sulfated compounds, where the activated sulfate, adenylyl-sulfate, is reduced to sulfite by the activity of adenylyl-sulfate reductase. |
| sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) | The pathway by which inorganic sulfate is processed and incorporated into sulfated compounds, where the phosphoadenylyl sulfate reduction step is catalyzed by the enzyme phosphoadenylyl-sulfate reductase (thioredoxin) (EC:1.8.4.8). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLSPHGGILQ | DLVARDAEKK | DRLLHEAQGL | PQWNLTARQL | CDIELILNGG | FSPLTGFLGK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EDYESVVQNS | RLTSGLLWTI | PITLDVDEEF | AKSVNLGERI | ALLQDDDIFV | AIITVSDIYT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PDKKVEADKV | FRGDEEHPAI | QYLNETAGDI | YLGGELEAIQ | LPAHYDYLNL | RKSPAALRAD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FATQQWDRVV | AFQTRNPMHR | AHRELTIRAA | KEHNAKVLLH | PVVGLTKPGD | IDYHTRIKVY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KEIVKRYPEG | IAQLALLPLA | MRMAGDREAV | WHAIIRKNYG | ATHFIVGRDH | AGPGTNSKGD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DFYGPYDAQV | LVESYKNELG | IEVVPFKLIT | YLPDKDIYLP | VDEIDGSVKT | LTISGTELRK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RLREGTDIPD | WFTYPEIVEI | LRQYNPPRYR | QGFVIVVNHE | NPKRIANALL | STFLQVGGGR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QYKIFDHQGQ | PQLLELIPDF | VKSGTGLIVT | SPLPSSVDAH | NIYELNTYPS | AHIKVSATEP |
| 490 | |||||
| VTEIVQKTVF | FLEDNKFFQF |