A0A537VDK7 · A0A537VDK7_9PROT

  • Protein
    Coenzyme A biosynthesis bifunctional protein CoaBC
  • Gene
    coaBC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
FMN (UniProtKB | Rhea| CHEBI:58210 )

Note: Binds 1 FMN per subunit.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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.

TypeIDPosition(s)Description
Binding site355CTP (UniProtKB | ChEBI)
Binding site365CTP (UniProtKB | ChEBI)
Binding site382-385CTP (UniProtKB | ChEBI)
Binding site402CTP (UniProtKB | ChEBI)
Binding site416CTP (UniProtKB | ChEBI)
Binding site420CTP (UniProtKB | ChEBI)
Binding site528-530substrate
Binding site541substrate
Binding site547substrate

GO annotations

AspectTerm
Cellular Componentphosphopantothenoylcysteine decarboxylase complex
Molecular FunctiondUTP diphosphatase activity
Molecular FunctionFMN binding
Molecular Functionmagnesium ion binding
Molecular Functionphosphopantothenate--cysteine ligase activity
Molecular Functionphosphopantothenoylcysteine decarboxylase activity
Biological Processcoenzyme A biosynthetic process
Biological ProcessdUMP biosynthetic process
Biological ProcessdUTP catabolic process
Biological Processpantothenate catabolic process
Biological Processregulation of DNA-templated transcription

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Coenzyme A biosynthesis bifunctional protein CoaBC
  • Alternative names
    • DNA/pantothenate metabolism flavoprotein
    • Phosphopantothenoylcysteine synthetase/decarboxylase
      (PPCS-PPCDC
      )

Including 2 domains:

  • Recommended name
    Phosphopantothenoylcysteine decarboxylase
  • EC number
  • Short names
    PPC decarboxylase
    ; PPC-DC
  • Alternative names
    • CoaC
  • Recommended name
    Phosphopantothenate--cysteine ligase
  • EC number
  • Alternative names
    • CoaB
    • Phosphopantothenoylcysteine synthetase
      (PPC synthetase
      ; PPC-S
      )

Gene names

    • Name
      coaBC
    • Synonyms
      dut
    • ORF names
      E6G75_11495

Organism names

Accessions

  • Primary accession
    A0A537VDK7

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-267Phosphopantothenoylcysteine decarboxylase
Domain2-40Antitoxin FitA-like ribbon-helix-helix
Domain82-253Flavoprotein
Domain263-446DNA/pantothenate metabolism flavoprotein C-terminal
Region268-608Phosphopantothenate--cysteine ligase
Domain479-607dUTPase-like

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 status
    Complete
  • Length
    608
  • Mass (Da)
    62,959
  • Last updated
    2019-10-16 v1
  • Checksum
    2B6BE9F4ED67C42A
MASITIRQLGDDLKRRLRLRAARNGRSMEDEARTILRDAASLEAGRIEARPEAPQRAAPRGRVVADTPARAAAGAHAAGTQHILLIIGGGIAAYKALDLIRRLKEHGLAVRCILTKAAQEFITPLSAGALSGERVFTDLFDPGSEFDVGHIRLAREVDLVVVAPATADLMAKLAGGHADDLASAVLVATDRKVLLAPAMNPHMWQHKATQRNLARLVEDGVALVGPNTGEMAEAGEAGIGRMAEPLEIAAAVVSLIGDGEGALKGKRVIVTSGPTHESIDPVRYIANRSSGKQGHAIAAAAAEAGAHVTLVSGPVNVPDPPGVAVVKVTTAQDMLAAVTKALPADVAVFAAAVADWRIAKPQANKIKKGAGGSPKLALTENPDILATVAHDARKRPRLVIGFAAETEHIVEHAKAKLARKGCDWILANDVSAAGGAMGGDRNTVHFVTAQGVESWPPQSKEEVARALVARMAETLAGAKRSAHAAGLDLVAAVPAGAPVIIAPGGRAAIPTGLAFALPAGIEGQIRPRSGLALHHGVTVLNSPGTLDPDYRGEVHVILANFGRDPFAVERGARIAQLVLAATLQAAIREVANLDETTRGVRGFGSTGT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VAZL01000307
EMBL· GenBank· DDBJ
TMK16428.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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