W9T363 · W9T363_9PSED
- ProteinCoenzyme A biosynthesis bifunctional protein CoaBC
- GenecoaBC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids403 (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 | 159 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 278 | CTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 288 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 307-310 | CTP (UniProtKB | ChEBI) | ||||
Sequence: PDIL | ||||||
Binding site | 325 | CTP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 339 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 343 | 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
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionW9T363
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-190 | Phosphopantothenoylcysteine decarboxylase | ||||
Sequence: MQRLYRKRIVLGVGGGIAAYKSAELVRRLRDHGAEVRVVMTQGGREFITPLTLQALSGHPVHLDLLDPAAEAAMGHIELARWADLVLVAPATADLMARLAQGTANDLLTTLVLATNAPVALAPAMNQAMWADPATQANRELLLERGIRLFGPGSGSQACGDVGMGRMLEAEELAQAAADCFATGTLTGLH | ||||||
Domain | 7-179 | Flavoprotein | ||||
Sequence: KRIVLGVGGGIAAYKSAELVRRLRDHGAEVRVVMTQGGREFITPLTLQALSGHPVHLDLLDPAAEAAMGHIELARWADLVLVAPATADLMARLAQGTANDLLTTLVLATNAPVALAPAMNQAMWADPATQANRELLLERGIRLFGPGSGSQACGDVGMGRMLEAEELAQAAAD | ||||||
Domain | 186-370 | DNA/pantothenate metabolism flavoprotein C-terminal | ||||
Sequence: LTGLHLLITAGPTQENIDPVRYITNHSSGKMGFALAEAAAEAGARVTLVTGPVFLPTPDRVQRIDVVSARDMLAACEAAMPCDLLVAAAAVADYRPEVVAPHKLKKDPNSGDGLLLQMVRNPDILATLASRPDRPFCVGFAAETENLLEYATRKLRDKNLDLIVANDVANPSIGFNSEDNAVSVI | ||||||
Region | 191-403 | Phosphopantothenate--cysteine ligase | ||||
Sequence: LLITAGPTQENIDPVRYITNHSSGKMGFALAEAAAEAGARVTLVTGPVFLPTPDRVQRIDVVSARDMLAACEAAMPCDLLVAAAAVADYRPEVVAPHKLKKDPNSGDGLLLQMVRNPDILATLASRPDRPFCVGFAAETENLLEYATRKLRDKNLDLIVANDVANPSIGFNSEDNAVSVIDRQQHETRFGQASKGHIARELVAFIADRYQKQA |
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.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length403
- Mass (Da)43,043
- Last updated2014-05-14 v1
- Checksum63862636FA7A9544
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AZSV01000035 EMBL· GenBank· DDBJ | EXF44893.1 EMBL· GenBank· DDBJ | Genomic DNA |