T2G899
Gene name |
aprB |
Protein name |
Adenylylsulfate reductase subunit beta |
Names |
AdoPSO(4) reductase subunit B, Adenosine 5'-phosphosulfate reductase subunit beta, APSR subunit B |
Species |
Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759) (Desulfovibrio gigas) |
KEGG Pathway |
dgg:DGI_0458 |
EC number |
|
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
2 structures for T2G899
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3GYX | X-ray | 320 A | B/D/F/H/J/L | 2-167 | PDB |
| AF-T2G899-F1 | Predicted | AlphaFoldDB |
No variants for T2G899
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for T2G899 | |||||
No associated diseases with T2G899
3 regional properties for T2G899
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. |
3 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. |
| metal ion binding | Binding to a metal ion. |
| protein heterodimerization activity | Binding to a nonidentical protein to form a heterodimer. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| dissimilatory sulfate reduction | The reduction of sulfate to hydrogen sulfide, which acts as a terminal electron acceptor. Sulfate is activated to adenosine-phosphosulfate (APS) which is then reduced to sulfite, which is in turn reduced to hydrogen sulfide. |
| protein heterotetramerization | The formation of a protein heterotetramer, a macromolecular structure consisting of four noncovalently associated subunits, of which not all are identical. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPTFVDPSKC | DGCKGGEKTA | CMYICPNDLM | ILDPEEMKAF | NQEPEACWEC | YSCIKICPQG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AITARPYADF | APMGGTCIPL | RGSEDIMWTI | KFRNGSVKRF | KFPIRTTPEG | SIKPFEGKPE |
| 130 | 140 | 150 | 160 | ||
| AGDLENELLF | TETALTVPQV | ALGQKAQIAD | AETSQCWFDL | PCEGGNR |