A0A6B9HER0 · PIPCL_PIPNI

Function

function

Involved in the biosynthesis of aromatic piperamides natural products such as piperine (1-piperoyl-piperidine), the pungent principle contributing, together with several terpenoids, to the aromatic properties of black pepper fruits, and displaying numerous pharmacological activities such as antiproliferative, antitumor, antiangiogenesis, antioxidant, antidiabetic, antiobesity, cardioprotective, antimicrobial, antiaging, and immunomodulatory effects (PubMed:31837062).
Acts as a carboxylate--CoA ligase that catalyzes exclusively the formation of piperoyl--CoA from piperic acid and CoA (PubMed:31837062).
Can also use the synthetic substrate 5-phenylpentanoic acid to form the corresponding CoA ester (PubMed:31837062).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
43.3 μMpiperic acid
24.3 μM5-phenylpentanoic acid
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
19.6 nmol/sec/mgwith piperic acid as substrate
27.9 nmol/sec/mgwith 5-phenylpentanoic acid as substrate
kcat is 1.09 sec-1 with piperic acid as substrate (PubMed:31837062).
kcat is 4.17 sec-1 with 5-phenylpentanoic acid as substrate (PubMed:31837062).

Pathway

Aromatic compound metabolism.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site203ATP (UniProtKB | ChEBI)
Binding site204ATP (UniProtKB | ChEBI)
Binding site205ATP (UniProtKB | ChEBI)
Binding site206ATP (UniProtKB | ChEBI)
Binding site207ATP (UniProtKB | ChEBI)
Binding site211ATP (UniProtKB | ChEBI)
Binding site272CoA (UniProtKB | ChEBI)
Binding site343ATP (UniProtKB | ChEBI)
Binding site344ATP (UniProtKB | ChEBI)
Binding site348ATP (UniProtKB | ChEBI)
Binding site428ATP (UniProtKB | ChEBI)
Binding site440-443ATP (UniProtKB | ChEBI)
Binding site451CoA (UniProtKB | ChEBI)
Binding site452CoA (UniProtKB | ChEBI)
Binding site534ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentperoxisome
Molecular FunctionATP binding
Molecular FunctionCoA-ligase activity
Molecular Functionlong-chain fatty acid-CoA ligase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Piperic acid--CoA ligase
  • EC number
  • Short names
    PipCoA ligase

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Magnoliidae > Piperales > Piperaceae > Piper

Accessions

  • Primary accession
    A0A6B9HER0

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Strongly reduced piperine content in fruits.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004569041-548Piperic acid--CoA ligase

Expression

Tissue specificity

Mostly expressed in immature green fruits, and, to a lower extent, in leaves and flowers.

Developmental stage

Highest levels observed in fruits 2 months post anthesis.

Interaction

Subunit

Monomer.

Family & Domains

Features

Showing features for region, motif.

TypeIDPosition(s)Description
Region274-343SBD1
Region344-407SBD2
Motif546-548Microbody targeting signal

Sequence similarities

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    548
  • Mass (Da)
    59,821
  • Last updated
    2020-06-17 v1
  • Checksum
    F78A25162AC49564
MEKSGYGNDGIYRSLRPPVLFPNDPNLSVTSYLFQRSDAYPDRLALADANSGETLNFAQFKAMVQRVSHGLSRLGIKKGDVVLIFSPNSIYFPVCFLAIVALGAVVTTGNPQYTSAEITKQANDSKPKLVITVPQLWDKVNHLGLPAVFLGSKISGDGTIAPSNRNINGTVTYFSNLVELGGHVSEFPPVSIKRSDIAALLYSSGTSGTSKGVILTHRNLISTACMTTSDQEFDGEDPNVFLCFLPMSHVFGLVIICYSQLMRGNSVVSVEKFDLEMVLRSVGKYRVTYLCVVPPVMIALAKQNWGKIYDLSSLKRIICGSAPLGKEVIEECAKNYPHVPIIQGYGLTESCGIASLEIPEGVREYGSSGILFPAVEAKIVHVENLTPLPPNQLGEIWIRGPNMMQGYLNNPQATKLTIDEQGWVHTGDLGYFNGEGRLSVVDRIKELIKCKGFQVAPAELEGLLLSHQEILDAVVIPYPDAEAGEVPIAYVVRALSSTLDEEAVKKFIAEQVAPFKRLRKVTFVNSVPKSASGKILRRELIAKVRSKI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MN729603
EMBL· GenBank· DDBJ
QGY72664.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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