W9T363 · W9T363_9PSED

  • Protein
    Coenzyme A biosynthesis bifunctional protein CoaBC
  • Gene
    coaBC
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

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.

Features

Showing features for active site, binding site.

TypeIDPosition(s)Description
Active site159Proton donor
Binding site278CTP (UniProtKB | ChEBI)
Binding site288CTP (UniProtKB | ChEBI)
Binding site307-310CTP (UniProtKB | ChEBI)
Binding site325CTP (UniProtKB | ChEBI)
Binding site339CTP (UniProtKB | ChEBI)
Binding site343CTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentphosphopantothenoylcysteine decarboxylase complex
Molecular FunctionFMN binding
Molecular Functionmetal ion binding
Molecular Functionphosphopantothenate--cysteine ligase activity
Molecular Functionphosphopantothenoylcysteine decarboxylase activity
Biological Processcoenzyme A biosynthetic process
Biological Processpantothenate catabolic process

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
    • ORF names
      BAY1663_02691

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BAY1663
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    W9T363

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-190Phosphopantothenoylcysteine decarboxylase
Domain7-179Flavoprotein
Domain186-370DNA/pantothenate metabolism flavoprotein C-terminal
Region191-403Phosphopantothenate--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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    403
  • Mass (Da)
    43,043
  • Last updated
    2014-05-14 v1
  • Checksum
    63862636FA7A9544
MQRLYRKRIVLGVGGGIAAYKSAELVRRLRDHGAEVRVVMTQGGREFITPLTLQALSGHPVHLDLLDPAAEAAMGHIELARWADLVLVAPATADLMARLAQGTANDLLTTLVLATNAPVALAPAMNQAMWADPATQANRELLLERGIRLFGPGSGSQACGDVGMGRMLEAEELAQAAADCFATGTLTGLHLLITAGPTQENIDPVRYITNHSSGKMGFALAEAAAEAGARVTLVTGPVFLPTPDRVQRIDVVSARDMLAACEAAMPCDLLVAAAAVADYRPEVVAPHKLKKDPNSGDGLLLQMVRNPDILATLASRPDRPFCVGFAAETENLLEYATRKLRDKNLDLIVANDVANPSIGFNSEDNAVSVIDRQQHETRFGQASKGHIARELVAFIADRYQKQA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AZSV01000035
EMBL· GenBank· DDBJ
EXF44893.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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