P0CY53
Gene name |
bchL |
Protein name |
Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein |
Names |
DPOR subunit L, LI-POR subunit L |
Species |
Rhodobacter capsulatus (Rhodopseudomonas capsulata) |
KEGG Pathway |
|
EC number |
1.3.7.7: With an iron-sulfur protein 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 P0CY53
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0CY53-F1 | Predicted | AlphaFoldDB |
No variants for P0CY53
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0CY53 | |||||
No associated diseases with P0CY53
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.7.7 | With an iron-sulfur protein as acceptor |
| 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 |
5 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. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| oxidoreductase activity, acting on iron-sulfur proteins as donors | Catalysis of an oxidation-reduction (redox) reaction in which an iron-sulfur protein acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor. |
| oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor | Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces an iron-sulfur protein. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| light-independent bacteriochlorophyll biosynthetic process | The chemical reactions and pathways resulting in the formation of a bacteriochlorophyll, which occur in the absence of light. Bacteriochlorophylls are any of the chlorophylls of photosynthetic bacteria; they differ structurally from the chlorophylls of higher plants. |
| photosynthesis, dark reaction | A complex cycle of enzyme-mediated reactions which catalyzes the reduction of carbon dioxide to sugar. As well as carbon dioxide the cycle requires reducing power in the form of reduced nicotinamide adenine dinucleotide phosphate (NADP) and chemical energy in the form of adenosine triphosphate (ATP). The reduced NADP (NADPH) and ATP are produced by the 'light' reactions. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSPRDDIPDL | KGFDGDGEGS | VQVHDSEDIG | LDVGGARVFS | VYGQGGIGKS | TTSSNLSAAF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLLGKRVLQI | GCDPKHDSTF | TLTGRLQETV | IDILKQVNFH | PEELRPEDYV | TEGFNGVMCV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EAGGPPAGTG | CGGYVVGQTV | KLLKQHHLLE | DTDVVVFDVL | GDVVCGGFAA | PLQHADRALI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VTANDFDSIY | AMNRIIAAVQ | AKSVNYKVRL | AGCVANRSRE | TNEVDRYCEA | ANFKRIAHMP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DLDSIRRSRL | KKRTLFEMDD | AEDVVMARAE | YIRLAETLWR | STGEPGLTPE | PLTDRHIFEL |
| LGFD |