A0A2Z6DX63 · A0A2Z6DX63_HYDTE
- ProteinCoproporphyrinogen-III oxidase
- GenehemN
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids464 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 62 | S-adenosyl-L-methionine 1 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 68 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 72 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 74-76 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: YCA | ||||||
Binding site | 75 | [4Fe-4S] cluster (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 119 | S-adenosyl-L-methionine 1 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 120-121 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Hydrogenophilia > Hydrogenophilales > Hydrogenophilaceae > Hydrogenophilus
Accessions
- Primary accessionA0A2Z6DX63
Proteomes
Subcellular Location
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 53-287 | Radical SAM core | ||||
Sequence: AGVQRPLSLYVHIPYCNTICYYCACNKIITKDHSRSSRYLDYLEREMALVDEKLTGSRTVAQLHFGGGTPTFLHESEMRRLWAAIRRTFTLIEHGEYSIEVDPRKVGREQVFLLRELGFNRMSIGVQDFDPVVQRAVNRVQSLEETQGVLEAARAAGFHSVSFDLIYGLPHQSVARFAKTLDAVIALAPDRLSLYSYAHLPRLFMPQRRIDEATLPSAAEKLAILKMAIERLTDA |
Sequence similarities
Belongs to the anaerobic coproporphyrinogen-III oxidase family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length464
- Mass (Da)52,585
- Last updated2018-10-10 v1
- Checksum3D1DDEFA4A4E80F9
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP018558 EMBL· GenBank· DDBJ | BBD76905.1 EMBL· GenBank· DDBJ | Genomic DNA |