P74132 · HEMN_SYNY3
- ProteinOxygen-independent coproporphyrinogen III oxidase
- GenehemN
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids466 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the heme and chlorophyll biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
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 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
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 | 150 | S-adenosyl-L-methionine 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 177 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 189 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 214 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 248 | S-adenosyl-L-methionine 2 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 334 | 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 | chlorophyll biosynthetic process | |
Biological Process | porphyrin-containing compound biosynthetic process | |
Biological Process | protoporphyrinogen IX biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameOxygen-independent coproporphyrinogen III oxidase
- EC number
- Short namesCPO
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Synechococcales > Merismopediaceae > Synechocystis
Accessions
- Primary accessionP74132
Proteomes
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Cells lacking this gene grow significantly slower than that of the wild-type under microoxic conditions, while they grow normally under aerobic conditions. Coproporphyrin-III is accumulated at a low but significant level in the mutant growing under microoxic conditions.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000109954 | 1-466 | Oxygen-independent coproporphyrinogen III oxidase | |||
Sequence: MTTTFPTVEFSAELLNKYNQGIPRYTSYPPATELNKEFDPSDFQTAINLGNYKKTPLSLYCHIPFCAKACYFCGCNTIITQHKPAVDPYLKAVAKQIALVAPLVDQQRPVQQLHWGGGTPNYLTLEQAEFLFNTITDAFPLAENAEISIEINPCYVDKDYIFALRQLGFNRISFGIQDFNSQVQQAVNRIQPEAMLFQVMDWIRQANFDSVNVDLIYGLPHQNLATFRETLRKTAQLNPDRIAVFNFAYVPWLKPVQKKMPESALPPAEEKLKIMQATIADLTEQGYVFIGMDHFAKPDDELAIAQRRGELHRNFQGYTTQPESDLLGFGITSISMLQDVYAQNHKTLKAFYNALDREVMPIEKGFKLSQDDLIRRTVIKELMCQFKLSAQELESKYNLGFDCDFNDYFAKELSALDVLEADGLLRRLGDGLEVTPRGRILIRNIAAVFDTYLQNKSKQQMFSRAI |
Proteomic databases
Expression
Induction
Induced under microoxic conditions.
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 51-285 | Radical SAM core | ||||
Sequence: NYKKTPLSLYCHIPFCAKACYFCGCNTIITQHKPAVDPYLKAVAKQIALVAPLVDQQRPVQQLHWGGGTPNYLTLEQAEFLFNTITDAFPLAENAEISIEINPCYVDKDYIFALRQLGFNRISFGIQDFNSQVQQAVNRIQPEAMLFQVMDWIRQANFDSVNVDLIYGLPHQNLATFRETLRKTAQLNPDRIAVFNFAYVPWLKPVQKKMPESALPPAEEKLKIMQATIADLTEQ |
Sequence similarities
Belongs to the anaerobic coproporphyrinogen-III oxidase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length466
- Mass (Da)53,161
- Last updated1997-02-01 v1
- ChecksumD49735A905A5C572
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BA000022 EMBL· GenBank· DDBJ | BAA18218.1 EMBL· GenBank· DDBJ | Genomic DNA |