P9WNE3 · CPFC_MYCTU
- ProteinCoproporphyrin III ferrochelatase
- GenecpfC
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids344 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457).
Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457).
Has weaker activity with coproporphyrin I, protoporphyrin IX, deuteroporphyrin, 2,4 hydroxyethyl and 2,4 disulfonate (PubMed:11948160, PubMed:25646457).
Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457).
Has weaker activity with coproporphyrin I, protoporphyrin IX, deuteroporphyrin, 2,4 hydroxyethyl and 2,4 disulfonate (PubMed:11948160, PubMed:25646457).
Miscellaneous
Was identified as a high-confidence drug target.
Catalytic activity
- Fe-coproporphyrin III + 2 H+ = coproporphyrin III + Fe2+This reaction proceeds in the backward direction.
Cofactor
Note: Binds 1 [2Fe-2S] cluster.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
10.5 μM | coproporphyrin III | |||||
720 μM | protoporphyrin IX |
kcat is 1.8 min-1 with coproporphyrin III as substrate. kcat is 0.8 min-1 with protoporphyrin IX as substrate.
Pathway
Porphyrin-containing compound metabolism; protoheme biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 52 | Fe-coproporphyrin III (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 113 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 116 | Fe-coproporphyrin III (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 172 | Fe2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 255 | Fe2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 316 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 325 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 330 | [2Fe-2S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | 2 iron, 2 sulfur cluster binding | |
Molecular Function | ferrochelatase activity | |
Molecular Function | metal ion binding | |
Biological Process | heme biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCoproporphyrin III ferrochelatase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Mycobacteriales > Mycobacteriaceae > Mycobacterium > Mycobacterium tuberculosis complex
Accessions
- Primary accessionP9WNE3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000175167 | 1-344 | Coproporphyrin III ferrochelatase | |||
Sequence: MQFDAVLLLSFGGPEGPEQVRPFLENVTRGRGVPAERLDAVAEHYLHFGGVSPINGINRTLIAELEAQQELPVYFGNRNWEPYVEDAVTAMRDNGVRRAAVFATSAWSGYSSCTQYVEDIARARRAAGRDAPELVKLRPYFDHPLFVEMFADAITAAAATVRGDARLVFTAHSIPTAADRRCGPNLYSRQVAYATRLVAAAAGYCDFDLAWQSRSGPPQVPWLEPDVTDQLTGLAGAGINAVIVCPIGFVADHIEVVWDLDHELRLQAEAAGIAYARASTPNADPRFARLARGLIDELRYGRIPARVSGPDPVPGCLSSINGQPCRPPHCVASVSPARPSAGSP |
Proteomic databases
Interaction
Structure
Sequence
- Sequence statusComplete
- Length344
- Mass (Da)37,144
- Last updated2014-04-16 v1
- Checksum17A5023246B670B6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL123456 EMBL· GenBank· DDBJ | CCP44245.1 EMBL· GenBank· DDBJ | Genomic DNA |