A0A257CSE7 · A0A257CSE7_9BURK

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 site162Proton donor
Binding site282CTP (UniProtKB | ChEBI)
Binding site292CTP (UniProtKB | ChEBI)
Binding site332CTP (UniProtKB | ChEBI)
Binding site346CTP (UniProtKB | ChEBI)
Binding site350CTP (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
      CFE43_13030

Organism names

Accessions

  • Primary accession
    A0A257CSE7

Proteomes

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-193Phosphopantothenoylcysteine decarboxylase
Domain7-181Flavoprotein
Domain189-373DNA/pantothenate metabolism flavoprotein C-terminal
Region194-409Phosphopantothenate--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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    409
  • Mass (Da)
    43,081
  • Last updated
    2017-12-20 v1
  • Checksum
    237A0D10DFAAB923
MNDLAGKHIVLGLTGGIACYKAAELCRALIKEGATVQVVMTEAAAQFITPVTLQALSNRTVYDSQWDARERNNMPHINLSREADAILIAPCSADFMAKLLHGRADDLLSLMCLARPIDSVPLLVAPAMNREMWAHPATQRNLAQLQADGATLLGVGSGFQACGETGDGRMLEPQELLQDVIAFFQPKVLAGEHVLVTAGPTFEAIDPVRGITNLSSGKMGFAIARAAQEAGATVTLVAGPVHLPTPRGVQRVDVKSAANMLVQAVDSAGAATIFVATAAVADWRPASTAEQKIKKDASGLLPALEFVENTDILATIAQSPRAQSGALYCVGFAAESHDLLQHATAKRIRKGVPLLVGNIGPATFGQDDNALLLVDADGATEIARNDKLTLARRLVAEIAQRRKAAANPA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NKIK01000022
EMBL· GenBank· DDBJ
OYT91439.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp