A2CBW9
Gene name |
pebB |
Protein name |
Phycoerythrobilin:ferredoxin oxidoreductase |
Names |
|
Species |
Prochlorococcus marinus (strain MIT 9303) |
KEGG Pathway |
pmf:P9303_22441 |
EC number |
1.3.7.3: 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 A2CBW9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2CBW9-F1 | Predicted | AlphaFoldDB |
No variants for A2CBW9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A2CBW9 | |||||
No associated diseases with A2CBW9
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.7.3 | 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 |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cobalt ion binding | Binding to a cobalt ion (Co). |
| phycoerythrobilin:ferredoxin oxidoreductase activity | Catalysis of the reaction: (3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin + reduced ferredoxin. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| phytochromobilin biosynthetic process | The chemical reactions and pathways resulting in the formation of phytochromobilin, which involves the oxidative cleavage of heme by a heme oxygenase(HO) to form biliverdin IX alpha. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKPLRLSSLD | PVRMPEWRWA | PFLSHAINAL | IPLKPEPYPV | APEFLQREGK | TGSKSQPIKV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TTCTWACRTK | KFRQVRAACV | EAGSSASVLN | FVINPYHTFD | LPFFGADLVT | LPSGHLLALD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LQPAITSDER | HTKQVWERLM | PIFEQWRVRL | PEGGPIPEEA | KPYFSPGFLW | TRLHLGSEGN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QLIDEVIMPA | FRDYLNLYLD | LVEMAEEVSP | QRAFKLLEGQ | KRYLSYRGKK | DPARAMLARF |
| 250 | |||||
| HGHQWTESYI | HNVLFDL |