A0A0U1MJB7 · A0A0U1MJB7_STAAU
- ProteinCoenzyme A biosynthesis bifunctional protein CoaBC
- GenecoaBC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids399 (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 | 154 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 280 | CTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 290 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 324 | CTP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 338 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 342 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K |
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
Enzyme and pathway databases
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
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus
Accessions
- Primary accessionA0A0U1MJB7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-191 | Phosphopantothenoylcysteine decarboxylase | ||||
Sequence: MKKILLAVTGGIAAYKAIDLTSKLTQSGYEVRVMLTNHAQKFVTPLAFQAISRNAVYTDTFIEENPSEIQHIALGDWADAIIVAPATANTIAKLSVGIADDLVTSTLLATETPKFIAPAMNVHMYENKRTQQNINILKEDGYHFIEPGSGFLACGYVAKGRMEEPLQIVSVIDAHFQNSNRLANSSFQDKR | ||||||
Domain | 2-173 | Flavoprotein | ||||
Sequence: KKILLAVTGGIAAYKAIDLTSKLTQSGYEVRVMLTNHAQKFVTPLAFQAISRNAVYTDTFIEENPSEIQHIALGDWADAIIVAPATANTIAKLSVGIADDLVTSTLLATETPKFIAPAMNVHMYENKRTQQNINILKEDGYHFIEPGSGFLACGYVAKGRMEEPLQIVSVID | ||||||
Domain | 188-368 | DNA/pantothenate metabolism flavoprotein C-terminal | ||||
Sequence: QDKRALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALRNRGAIVTLVTGPTTLEDPKDIEVIHVQSAEEMFEQVTSRFDEQDIVVKAAAVSDYTPVDVLEHKMKKQDGDLSVSFKRTKDILKYLGEHKTSQYLIGFAAETEDIENYAQQKLRKKNADVIISNNVGDMSIGFSSDDNELTM | ||||||
Region | 192-399 | Phosphopantothenate--cysteine ligase | ||||
Sequence: ALVTAGPTIEVIDPVRFVSNRSSGKMGYAIAEALRNRGAIVTLVTGPTTLEDPKDIEVIHVQSAEEMFEQVTSRFDEQDIVVKAAAVSDYTPVDVLEHKMKKQDGDLSVSFKRTKDILKYLGEHKTSQYLIGFAAETEDIENYAQQKLRKKNADVIISNNVGDMSIGFSSDDNELTMHFKNNEKVNIKKGKKVVLAAQILDELETRWQ |
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
- Length399
- Mass (Da)44,170
- Last updated2016-02-17 v1
- ChecksumDDC816BF63F3350E
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CVOQ01000017 EMBL· GenBank· DDBJ | CRI09361.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WPRH01000386 EMBL· GenBank· DDBJ | MVI55422.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
WPVZ01000743 EMBL· GenBank· DDBJ | MVL46566.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
PGWZ01000409 EMBL· GenBank· DDBJ | PPJ73075.1 EMBL· GenBank· DDBJ | Genomic DNA |