B7LXG4
Gene name |
cysD |
Protein name |
Sulfate adenylyltransferase subunit 2 |
Names |
ATP-sulfurylase small subunit, Sulfate adenylate transferase, SAT |
Species |
Escherichia coli O8 (strain IAI1) |
KEGG Pathway |
ecr:ECIAI1_2854 |
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 B7LXG4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B7LXG4-F1 | Predicted | AlphaFoldDB |
No variants for B7LXG4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B7LXG4 | |||||
No associated diseases with B7LXG4
16 regional properties for B7LXG4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Flavodoxin-like | 65 - 78 | IPR001094-1 |
| domain | Flavodoxin-like | 113 - 124 | IPR001094-2 |
| domain | Flavodoxin-like | 145 - 155 | IPR001094-3 |
| domain | Flavodoxin-like | 169 - 188 | IPR001094-4 |
| domain | Oxidoreductase FAD/NAD(P)-binding | 459 - 565 | IPR001433 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 272 - 282 | IPR001709-1 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 388 - 395 | IPR001709-2 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 421 - 430 | IPR001709-3 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 458 - 477 | IPR001709-4 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 483 - 492 | IPR001709-5 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 496 - 507 | IPR001709-6 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 527 - 543 | IPR001709-7 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 550 - 558 | IPR001709-8 |
| domain | Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding | 232 - 426 | IPR003097 |
| domain | Flavodoxin/nitric oxide synthase | 64 - 202 | IPR008254 |
| domain | FAD-binding domain, ferredoxin reductase-type | 236 - 450 | IPR017927 |
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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
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. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| hydrogen sulfide biosynthetic process | The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S. |
| sulfate assimilation | The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds. |
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDQIRLTHLR | QLEAESIHII | REVAAEFSNP | VMLYSIGKDS | SVMLHLARKA | FYPGTLPFPL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LHVDTGWKFR | EMYEFRDRTA | KAYGCELLVH | KNPEGVAMGI | NPFVHGSAKH | TDIMKTEGLK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QALNKYGFDA | AFGGARRDEE | KSRAKERIYS | FRDRFHRWDP | KNQRPELWHN | YNGQINKGES |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IRVFPLSNWT | EQDIWQYIWL | ENIDIVPLYL | AAERPVLERD | GMLMMIDDNR | IDLQPGEVIK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KRMVRFRTLG | CWPLTGAVES | NAQTLPEIIE | EMLVSTTSER | QGRVIDRDQA | GSMELKKRQG |
| YF |