Protein profile
KP13_02740
Oxygen-independent coproporphyrinogen-III oxidase-like protein
Genome: KpKP13
Overview
Basic information about this protein and its source genome.
- Accession
- KP13_02740
- Gene
- AHE42692.1
- Status
- annotated
- Amino acids
- 378
- Structure source
- AlphaFold + ColabFold
Target profile
Computed evidence for target prioritization.
- Human off-target
- hit
- Human identity (%)
- 36.42
- Human E-value
- 5.92e-19
- Gut microbiome off-target
- hit
- Essential (DEG)
- N
- DEG identity (%)
- 0.0
- Localization
- Cytoplasmic
- ColabFold pLDDT
- 96.08
Selected Druggability evidence
AlphaFold / UniProt modelSelected Druggability is the FPocket score chosen for ranking using the curated structure priority. The 3D viewer may show a different loaded structure, so its visible pockets can differ.
Sequence
Primary amino-acid sequence viewer.
Functional Annotations
Enzyme classification and Gene Ontology terms linked to this protein.
Gene Ontology (GO)
7- GO:0051539 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.
- GO:0004109 Catalysis of the reaction: coproporphyrinogen III + 2 H+ + O2 = 2 CO2 + 2 H2O + protoporphyrinogen IX.
- GO:0005737 The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
- GO:0003824 Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic.
- GO:0006779 The chemical reactions and pathways resulting in the formation of any member of a large group of derivatives or analogs of porphyrin. Porphyrin consists of a ring of four pyrrole nuclei linked each to the next at their alpha positions through a methine group.
- GO:0051536 Binding to an iron-sulfur cluster, a combination of iron and sulfur atoms.
- GO:0046872 Binding to a metal ion.
Sequence Features
Domain/signature hits from InterPro and related databases.
Show feature table
| Start | End | DB | Term | Name |
|---|---|---|---|---|
| 2 | 376 | SFLD | SFLDF00288 | HemN-like, clustered with nucleoside-triphosphate RdgB |
| 9 | 219 | Gene3D | G3DSA:3.20.20.70 | Aldolase class I |
| 9 | 219 | InterPro | IPR013785 | Aldolase-type TIM barrel |
| 6 | 377 | PANTHER | PTHR13932 | COPROPORPHYRINIGEN III OXIDASE |
| 6 | 377 | InterPro | IPR034505 | Anaerobic coproporphyrinogen-III oxidase |
| 16 | 241 | SFLD | SFLDG01082 | B12-binding domain containing |
| 9 | 222 | FunFam | G3DSA:3.20.20.70:FF:000124 | Heme chaperone HemW |
| 5 | 376 | SUPERFAMILY | SSF102114 | Radical SAM enzymes |
| 2 | 376 | SFLD | SFLDG01065 | anaerobic coproporphyrinogen-III oxidase like |
| 15 | 216 | CDD | cd01335 | Radical_SAM |
| 1 | 237 | ProSiteProfiles | PS51918 | Radical SAM core domain profile. |
| 1 | 237 | InterPro | IPR007197 | Radical SAM |
| 7 | 368 | NCBIfam | TIGR00539 | radical SAM family heme chaperone HemW |
| 7 | 368 | InterPro | IPR004559 | Heme chaperone HemW-like |
| 11 | 179 | Pfam | PF04055 | Radical SAM superfamily |
| 11 | 179 | InterPro | IPR007197 | Radical SAM |
| 6 | 376 | SFLD | SFLDF00562 | HemN-like, clustered with heat shock genes |
| 6 | 376 | InterPro | IPR004559 | Heme chaperone HemW-like |
| 304 | 364 | Pfam | PF06969 | HemN C-terminal domain |
| 304 | 364 | InterPro | IPR010723 | HemN, C-terminal |
| 6 | 223 | SMART | SM00729 | MiaB |
| 6 | 223 | InterPro | IPR006638 | Elp3/MiaA/NifB-like, radical SAM core domain |
3D Structure
Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.
Loading 3D structure...
Structural evidence
0 + 2Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.
| Entry | Method | Resolution | Chain | Coverage | Links | Status |
|---|---|---|---|---|---|---|
|
AlphaFold
AF_A0A0H3GXJ4
|
AlphaFold | — | — | full sequence | — | Viewing |
|
ColabFold
KP13_02740
|
ColabFold | — | — | full sequence | — | Loaded |
Pocket details FPocket · P2Rank — toggle visibility and zoom from here, or open full viewer
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 2 | 0.781 | ||||||
| 1 | 0.494 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 46.69 | 0.975 | ||||||
| 2 | 1.82 | 0.035 | ||||||
| 3 | 0.95 | 0.005 |
Pockets (FPOCKET)
Showing top-ranked FPocket candidates by druggability. Druggability is color-coded: high (0.7 or higher), medium (0.4 to 0.69), low (below 0.4).
| FPOCKET | Sticks | Spheres | Surfaces | Druggability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|
| 13 | 0.578 |
Pockets (P2RANK)
Showing top-ranked P2Rank candidates by probability. Probability is color-coded per P2Rank calibration: high (≥ 0.5), medium (0.2 – 0.49), low (< 0.2).
| P2RANK | Sticks | Spheres | Surfaces | Score | Probability | Labels | Zoom | Positions |
|---|---|---|---|---|---|---|---|---|
| 1 | 45.09 | 0.972 | ||||||
| 2 | 1.05 | 0.006 |