Q5X5U7
Gene name |
hemF |
Protein name |
Oxygen-dependent coproporphyrinogen-III oxidase |
Names |
CPO, Coprogen oxidase, Coproporphyrinogenase |
Species |
Legionella pneumophila (strain Paris) |
KEGG Pathway |
lpp:lpp1223 |
EC number |
1.3.3.3: With oxygen 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 Q5X5U7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5X5U7-F1 | Predicted | AlphaFoldDB |
No variants for Q5X5U7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5X5U7 | |||||
No associated diseases with Q5X5U7
4 regional properties for Q5X5U7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase | 162 - 276 | IPR006151 |
| domain | Glutamyl-tRNA reductase, N-terminal | 33 - 139 | IPR015895 |
| domain | Tetrapyrrole biosynthesis, glutamyl-tRNA reductase, dimerisation domain | 294 - 381 | IPR015896 |
| conserved_site | Glutamyl-tRNA reductase, conserved site | 82 - 105 | IPR018214 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.3.3 | With oxygen 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| coproporphyrinogen oxidase activity | Catalysis of the reaction: coproporphyrinogen III + 2 H(+) + O(2) = 2 CO(2) + 2 H(2)O + protoporphyrinogen IX. |
| metal ion binding | Binding to a metal ion. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protoporphyrinogen IX biosynthetic process | The chemical reactions and pathways resulting in the formation of protoporphyrinogen IX. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSISKTLPYN | AIEQIKSYLL | QLQNTICVLL | ESIDGKTRFH | EDSWQRAAGG | GGRTRIMTNG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NVFEKAGVNF | SHVSGEQLPA | SASAHREELA | GRHFSALGVS | LVIHPQNPYV | PTTHANVRFF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VAEKEDSEPV | WWFGGGFDLT | PYYGFVEDCE | HWHQTALNAC | LPFGETIYPK | FKRWCDDYFF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IKHRNEARGI | GGLFFDDYNE | ISFDHSFELM | RSIGDHFILA | YEPIVARRKD | IPFGNREKAF |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QNYRRGRYAE | FNLVYDRGTL | FGLQSGGRTE | SILMSLPPTV | HWEYNWHPEK | GSDEEKLYTD |
| 310 | |||||
| FLPAKDWLKK | E |