A0A537VDK7 · A0A537VDK7_9PROT
- ProteinCoenzyme A biosynthesis bifunctional protein CoaBC
- GenecoaBC
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids608 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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.
This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
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.
Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 355 | CTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 365 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 382-385 | CTP (UniProtKB | ChEBI) | ||||
Sequence: PDIL | ||||||
Binding site | 402 | CTP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 416 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 420 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 528-530 | substrate | ||||
Sequence: RSG | ||||||
Binding site | 541 | substrate | ||||
Sequence: N | ||||||
Binding site | 547 | substrate | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | phosphopantothenoylcysteine decarboxylase complex | |
Molecular Function | dUTP diphosphatase activity | |
Molecular Function | FMN binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphopantothenate--cysteine ligase activity | |
Molecular Function | phosphopantothenoylcysteine decarboxylase activity | |
Biological Process | coenzyme A biosynthetic process | |
Biological Process | dUMP biosynthetic process | |
Biological Process | dUTP catabolic process | |
Biological Process | pantothenate catabolic process | |
Biological Process | regulation of DNA-templated transcription |
Keywords
- Molecular function
- Biological process
- 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 > Alphaproteobacteria
Accessions
- Primary accessionA0A537VDK7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-267 | Phosphopantothenoylcysteine decarboxylase | ||||
Sequence: MASITIRQLGDDLKRRLRLRAARNGRSMEDEARTILRDAASLEAGRIEARPEAPQRAAPRGRVVADTPARAAAGAHAAGTQHILLIIGGGIAAYKALDLIRRLKEHGLAVRCILTKAAQEFITPLSAGALSGERVFTDLFDPGSEFDVGHIRLAREVDLVVVAPATADLMAKLAGGHADDLASAVLVATDRKVLLAPAMNPHMWQHKATQRNLARLVEDGVALVGPNTGEMAEAGEAGIGRMAEPLEIAAAVVSLIGDGEGALKGKR | ||||||
Domain | 2-40 | Antitoxin FitA-like ribbon-helix-helix | ||||
Sequence: ASITIRQLGDDLKRRLRLRAARNGRSMEDEARTILRDAA | ||||||
Domain | 82-253 | Flavoprotein | ||||
Sequence: HILLIIGGGIAAYKALDLIRRLKEHGLAVRCILTKAAQEFITPLSAGALSGERVFTDLFDPGSEFDVGHIRLAREVDLVVVAPATADLMAKLAGGHADDLASAVLVATDRKVLLAPAMNPHMWQHKATQRNLARLVEDGVALVGPNTGEMAEAGEAGIGRMAEPLEIAAAVV | ||||||
Domain | 263-446 | DNA/pantothenate metabolism flavoprotein C-terminal | ||||
Sequence: LKGKRVIVTSGPTHESIDPVRYIANRSSGKQGHAIAAAAAEAGAHVTLVSGPVNVPDPPGVAVVKVTTAQDMLAAVTKALPADVAVFAAAVADWRIAKPQANKIKKGAGGSPKLALTENPDILATVAHDARKRPRLVIGFAAETEHIVEHAKAKLARKGCDWILANDVSAAGGAMGGDRNTVHF | ||||||
Region | 268-608 | Phosphopantothenate--cysteine ligase | ||||
Sequence: VIVTSGPTHESIDPVRYIANRSSGKQGHAIAAAAAEAGAHVTLVSGPVNVPDPPGVAVVKVTTAQDMLAAVTKALPADVAVFAAAVADWRIAKPQANKIKKGAGGSPKLALTENPDILATVAHDARKRPRLVIGFAAETEHIVEHAKAKLARKGCDWILANDVSAAGGAMGGDRNTVHFVTAQGVESWPPQSKEEVARALVARMAETLAGAKRSAHAAGLDLVAAVPAGAPVIIAPGGRAAIPTGLAFALPAGIEGQIRPRSGLALHHGVTVLNSPGTLDPDYRGEVHVILANFGRDPFAVERGARIAQLVLAATLQAAIREVANLDETTRGVRGFGSTGT | ||||||
Domain | 479-607 | dUTPase-like | ||||
Sequence: KRSAHAAGLDLVAAVPAGAPVIIAPGGRAAIPTGLAFALPAGIEGQIRPRSGLALHHGVTVLNSPGTLDPDYRGEVHVILANFGRDPFAVERGARIAQLVLAATLQAAIREVANLDETTRGVRGFGSTG |
Sequence similarities
Belongs to the dUTPase family.
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
- Length608
- Mass (Da)62,959
- Last updated2019-10-16 v1
- Checksum2B6BE9F4ED67C42A