B9DKR5
Gene name |
chdC |
Protein name |
Coproheme decarboxylase |
Names |
Coproheme III oxidative decarboxylase, Hydrogen peroxide-dependent heme synthase |
Species |
Staphylococcus carnosus (strain TM300) |
KEGG Pathway |
sca:SCA_0241 |
EC number |
1.3.98.5: With other, known, 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 B9DKR5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B9DKR5-F1 | Predicted | AlphaFoldDB |
No variants for B9DKR5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B9DKR5 | |||||
No associated diseases with B9DKR5
No regional properties for B9DKR5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for B9DKR5 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.98.5 | With other, known, acceptors |
| 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 |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| metal ion binding | Binding to a metal ion. |
| peroxidase activity | Catalysis of the reaction: a donor + a peroxide = an oxidized donor + 2 H2O. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| heme biosynthetic process | The chemical reactions and pathways resulting in the formation of heme, any compound of iron complexed in a porphyrin (tetrapyrrole) ring, from less complex precursors. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSQAAETLDG | WYSLHLFYAV | DWPTLRLVPD | EDRIQIVQEF | HDFLDKLASV | RDDHNGDHAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YNITGQKADI | LLWVLRPEMQ | ELNSIELALN | KLRIADYLVP | TYSYVSIIEL | SNYLAGKSDE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DPYENPHVKA | RLYPELPHSD | YICFYPMNKR | RNETYNWYML | SMEERQKLMY | DHGMIGRKYA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GKIKQFITGS | VGFDDYEWGV | TLFAQDPLQF | KKIVYEMRFD | ETTARYGDFG | SFFVGHVLPE |
| ETLETFFRI |