A0A1J9PKJ4 · A0A1J9PKJ4_9BURK
- ProteinCoproporphyrinogen-III oxidase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids463 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
Catalytic activity
- coproporphyrinogen III + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + 2 CO2 + 2 L-methionine + protoporphyrinogen IX
Cofactor
Note: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Pathway
Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (AdoMet route): step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 60 | S-adenosyl-L-methionine 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 66 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 70 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 72-74 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: YCG | ||||||
Binding site | 73 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 117 | S-adenosyl-L-methionine 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 118-119 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: GT | ||||||
Binding site | 152 | S-adenosyl-L-methionine 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 179 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 191 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 216 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 250 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 336 | S-adenosyl-L-methionine 1 (UniProtKB | ChEBI) | ||||
Sequence: I |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | coproporphyrinogen dehydrogenase activity | |
Molecular Function | coproporphyrinogen oxidase activity | |
Molecular Function | metal ion binding | |
Biological Process | protoporphyrinogen IX biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCoproporphyrinogen-III oxidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Burkholderiaceae > Burkholderia > Burkholderia cepacia complex
Accessions
- Primary accessionA0A1J9PKJ4
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 51-284 | Radical SAM core | ||||
Sequence: GASSSELSLYFHIPFCNTACFYCGCNKIATNNRRRARPYLDQLKREMALQAALFDPARPVTQLHWGGGTPTFLSDDETAELMAATREHFALAPDADAEFSIEIDPRTVTPASLVHLRTIGFNRLSLGVQDFDPVVQQAINRIQPLAMTADLLGAARATGFHSVSVDLIYGLPHQTVSVFARTLETIIELAPDRLSVFGYAHMPHLFKMQRQIDDATLPPPATRIALLGLAIDML |
Sequence similarities
Belongs to the anaerobic coproporphyrinogen-III oxidase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length463
- Mass (Da)51,069
- Last updated2017-02-15 v1
- ChecksumA6A482EC5484903F