A1B8C2
Gene name |
ctaA |
Protein name |
Heme A synthase |
Names |
HAS, Cytochrome aa3-controlling protein |
Species |
Paracoccus denitrificans (strain Pd 1222) |
KEGG Pathway |
pde:Pden_3699 |
EC number |
1.17.99.9: With other acceptors |
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 A1B8C2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1B8C2-F1 | Predicted | AlphaFoldDB |
No variants for A1B8C2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1B8C2 | |||||
No associated diseases with A1B8C2
2 regional properties for A1B8C2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Calreticulin/calnexin, conserved site | 130 - 138 | IPR018124-1 |
| conserved_site | Calreticulin/calnexin, conserved site | 243 - 255 | IPR018124-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.17.99.9 | With other acceptors |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor | Catalysis of an oxidation-reduction (redox) reaction in which NADH or NADPH acts as a hydrogen or electron donor and reduces a heme protein. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| heme A biosynthetic process | The chemical reactions and pathways resulting in the formation of heme A, a derivative of heme found in cytochrome aa3. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MARRPVFQEV | TETTPPGTTP | SGGMIDAGHK | GARGAIRLWL | VVLFVMVAAM | IALGGATRLT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GSGLSITEWK | PVTGAIPPMD | AATWQAEFDK | YRQIPQFELV | NSDMDLASFK | RIYWWEWSHR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LLGRLVGLVW | AAGFVFFLAT | RRIPTGWTPR | LLLLGALGGA | QGAIGWWMVH | SGLSGEMVRV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ASYRLATHLG | LAFAILGLIA | WYVLALSRSE | AALLRARRAG | EAKLFSMTTG | LMHLAFVQIL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LGALVAGIDA | GRMYTGWPTM | GGEWIPAEIW | DATLGWRNFF | ENPALVQFIH | RMTGYLLAVF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AVVVFLRARR | SPHPVTRGAY | VAMLVALAVQ | VALGIMNVLH | ASPLPLALAH | QIGAVALFTL |
| 370 | 380 | ||||
| ILRARHHARY | PYETSVRGTV | R |