Q5WKF5
Gene name |
cysH |
Protein name |
Adenosine 5'-phosphosulfate reductase |
Names |
APS reductase, 5'-adenylylsulfate reductase, Thioredoxin-dependent 5'-adenylylsulfate reductase |
Species |
Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii) |
KEGG Pathway |
bcl:ABC0611 |
EC number |
1.8.4.10: With a disulfide as acceptor |
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 Q5WKF5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5WKF5-F1 | Predicted | AlphaFoldDB |
No variants for Q5WKF5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5WKF5 | |||||
No associated diseases with Q5WKF5
1 regional properties for Q5WKF5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphoadenosine phosphosulphate reductase | 29 - 257 | IPR002500 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.8.4.10 | With a disulfide as acceptor |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to 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. |
| adenylyl-sulfate reductase (thioredoxin) activity | Catalysis of the reaction: AMP + sulfite + thioredoxin disulfide = 5'-adenylyl sulfate + thioredoxin. |
| metal ion binding | Binding to a metal ion. |
| 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 as PAPS. |
2 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. |
| 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 |
| MAYVFEQMEA | TDYEKVNTKL | KNRDSLDILR | WANQTYGEKL | VYACSFGAEA | MVLLDLLSKI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QKEAHILFLD | TDFHFAETYE | LIERVKERYP | TFRINMAKPA | LSPEEQAERY | GDELWLKNPD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QCCQIRKLDV | LARELEPYDA | WLSGLRREQS | PTRANTEFVN | QDKRFKKVKV | CPLIHWTEEE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IWMYIKLHQL | PYNELHDQHY | PSIGCTYCTK | AVMPGEDARS | GRWAGTGKTE | CGLHAPTKGD |
| S |