A0A9E4JLJ7 · A0A9E4JLJ7_9CYAN
- ProteinCoenzyme A biosynthesis bifunctional protein CoaBC
- GenecoaBC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids419 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalytic activity
- (R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H+
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FMN per subunit.
Pathway
Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 164 | Proton donor | |||
Binding site | 299 | CTP (UniProtKB | ChEBI) | |||
Binding site | 309 | CTP (UniProtKB | ChEBI) | |||
Binding site | 344 | CTP (UniProtKB | ChEBI) | |||
Binding site | 358 | CTP (UniProtKB | ChEBI) | |||
Binding site | 362 | CTP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | phosphopantothenoylcysteine decarboxylase complex | |
Molecular Function | FMN binding | |
Molecular Function | metal ion binding | |
Molecular Function | phosphopantothenate--cysteine ligase activity | |
Molecular Function | phosphopantothenoylcysteine decarboxylase activity | |
Biological Process | coenzyme A biosynthetic process | |
Biological Process | pantothenate catabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCoenzyme A biosynthesis bifunctional protein CoaBC
- Alternative names
Including 2 domains:
- Recommended namePhosphopantothenoylcysteine decarboxylase
- EC number
- Short namesPPC decarboxylase ; PPC-DC
- Alternative names
- Recommended namePhosphopantothenate--cysteine ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Oscillatoriophycideae > Oscillatoriales > Sirenicapillariaceae > Limnoraphis
Accessions
- Primary accessionA0A9E4JLJ7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 1-207 | Phosphopantothenoylcysteine decarboxylase | |||
Domain | 10-191 | Flavoprotein | |||
Domain | 204-389 | DNA/pantothenate metabolism flavoprotein C-terminal | |||
Region | 208-419 | Phosphopantothenate--cysteine ligase | |||
Sequence similarities
In the C-terminal section; belongs to the PPC synthetase family.
In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length419
- Mass (Da)45,271
- Last updated2023-05-03 v1
- Checksum3E5866A77B14A5DE
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAGTJT010000001 EMBL· GenBank· DDBJ | MCG5059373.1 EMBL· GenBank· DDBJ | Genomic DNA |