A0A2T5IGV8 · A0A2T5IGV8_9PROT

  • 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.

Type
IDPosition(s)Description
Active site151Proton donor
Binding site271CTP (UniProtKB | ChEBI)
Binding site281CTP (UniProtKB | ChEBI)
Binding site297-300CTP (UniProtKB | ChEBI)
Binding site315CTP (UniProtKB | ChEBI)
Binding site329CTP (UniProtKB | ChEBI)
Binding site333CTP (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
      C8R21_10276

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Nl12
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Nitrosomonadales > Nitrosomonadaceae > Nitrosospira

Accessions

  • Primary accession
    A0A2T5IGV8

Proteomes

Family & Domains

Features

Showing features for region, domain.

Type
IDPosition(s)Description
Region1-182Phosphopantothenoylcysteine decarboxylase
Domain2-168Flavoprotein
Domain178-352DNA/pantothenate metabolism flavoprotein C-terminal
Region183-396Phosphopantothenate--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
    396
  • Mass (Da)
    42,573
  • Last updated
    2018-07-18 v1
  • Checksum
    8389A0133DE6075D
MLLGLTGGVAAYKAAELARLLISDGLEVQAVMTASACRFVGTATLQALTGRPVFTELWDASVANNMAHIDLSRNVDAIVIAPASADFIAKVAHGRADDLLSTLCLARACPLLIAPSMNRQMWENPATQRNLRTLRRDGVTVLGPASGVQACGETGMGRMLEAHELAEAVHVFFQPKPLEAKRVLITAGPTFEAIDAVRGITNSSSGKMGYAVARAAVEAGAEVILISGPVCLEAPPAARLVRVTSAQDMLVAVKNETPHADFFISVAAVADYRPKSASEHKTKKNDRNIMLELVPNPDILEYVANLPDPPFCIGFAAETQNLEENAEAKRRRKKLPLLAANLAQEAIGAEEVALTLFDDSGKHPLPKSSKIEQARRLIEHAVPLYDKWQNFNSCKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QAOK01000002
EMBL· GenBank· DDBJ
PTQ83073.1
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