F0T8L4 · F0T8L4_METLA

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

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.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site262CTP (UniProtKB | ChEBI)
Binding site272CTP (UniProtKB | ChEBI)
Binding site305CTP (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
    • Ordered locus names
      Metbo_0304

Organism names

  • Taxonomic identifier
  • Strain
    • AL-21
  • Taxonomic lineage
    Archaea > Euryarchaeota > Methanomada group > Methanobacteria > Methanobacteriales > Methanobacteriaceae > Methanobacterium

Accessions

  • Primary accession
    F0T8L4

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain1-158Flavoprotein
Region1-173Phosphopantothenoylcysteine decarboxylase
Domain169-354DNA/pantothenate metabolism flavoprotein C-terminal
Region174-381Phosphopantothenate--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
    381
  • Mass (Da)
    41,667
  • Last updated
    2011-05-03 v1
  • Checksum
    975849501D14799A
MEIVLCVTGSIAATECVKLARELKRQGFDVKCFMSEDACNIIHPNAMEFATGQKVVTELTGDIEHVKYAQTDLILVAPATANIISKFAYKMADNPISTLLITGFGYQTPTVFVPSMHESMYRAVSQNIDGLKEEGILFLEPKREEGKAKFPDINDIVLQALRETSEGKLRGKKVLISAGGTYEAIDSVRGITNMSSGKMGLEIAREAFIQGADVTMVNGRVDVPIPSLFERFDVTSASEMINKLTDLLPENDIFISAAAVSDFKLECSDSQKISSDDDLIIHFKPGPKILNMVKELNPNIFLVGFKAESNISEEELVISARKQIEKSGADFVVANDISIEGSGFGSEKNQVVIVDDDTSSVPLCSKQEVAKKIVEKIIERV

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002551
EMBL· GenBank· DDBJ
ADZ08556.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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