A0A6B9HER0 · PIPCL_PIPNI
- ProteinPiperic acid--CoA ligase
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids548 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- a carboxylate + ATP + CoA = AMP + an acyl-CoA + diphosphateThis reaction proceeds in the forward direction.
- (E,E)-piperate + ATP + CoA = (E,E)-piperoyl-CoA + AMP + diphosphateThis reaction proceeds in the forward direction.
- (E,E)-piperate + ATP + H+ = (E,E)-piperoyl-AMP + diphosphateThis reaction proceeds in the forward direction.
- (E,E)-piperoyl-AMP + CoA = (E,E)-piperoyl-CoA + AMP + H+This reaction proceeds in the forward direction.
Cofactor
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
43.3 μM | piperic acid | |||||
24.3 μM | 5-phenylpentanoic acid |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
19.6 nmol/sec/mg | with piperic acid as substrate | ||||
27.9 nmol/sec/mg | with 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).
kcat is 4.17 sec-1 with 5-phenylpentanoic acid as substrate (PubMed:31837062).
Pathway
Aromatic compound metabolism.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 203 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 204 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 205 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 206 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 207 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 211 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 272 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 343 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 344 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 348 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 428 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 440-443 | ATP (UniProtKB | ChEBI) | ||||
Sequence: VVDR | ||||||
Binding site | 451 | CoA (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 452 | CoA (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 534 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | peroxisome | |
Molecular Function | ATP binding | |
Molecular Function | CoA-ligase activity | |
Molecular Function | long-chain fatty acid-CoA ligase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePiperic acid--CoA ligase
- EC number
- Short namesPipCoA ligase
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Magnoliidae > Piperales > Piperaceae > Piper
Accessions
- Primary accessionA0A6B9HER0
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Strongly reduced piperine content in fruits.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000456904 | 1-548 | Piperic acid--CoA ligase | |||
Sequence: MEKSGYGNDGIYRSLRPPVLFPNDPNLSVTSYLFQRSDAYPDRLALADANSGETLNFAQFKAMVQRVSHGLSRLGIKKGDVVLIFSPNSIYFPVCFLAIVALGAVVTTGNPQYTSAEITKQANDSKPKLVITVPQLWDKVNHLGLPAVFLGSKISGDGTIAPSNRNINGTVTYFSNLVELGGHVSEFPPVSIKRSDIAALLYSSGTSGTSKGVILTHRNLISTACMTTSDQEFDGEDPNVFLCFLPMSHVFGLVIICYSQLMRGNSVVSVEKFDLEMVLRSVGKYRVTYLCVVPPVMIALAKQNWGKIYDLSSLKRIICGSAPLGKEVIEECAKNYPHVPIIQGYGLTESCGIASLEIPEGVREYGSSGILFPAVEAKIVHVENLTPLPPNQLGEIWIRGPNMMQGYLNNPQATKLTIDEQGWVHTGDLGYFNGEGRLSVVDRIKELIKCKGFQVAPAELEGLLLSHQEILDAVVIPYPDAEAGEVPIAYVVRALSSTLDEEAVKKFIAEQVAPFKRLRKVTFVNSVPKSASGKILRRELIAKVRSKI |
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.
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 274-343 | SBD1 | ||||
Sequence: DLEMVLRSVGKYRVTYLCVVPPVMIALAKQNWGKIYDLSSLKRIICGSAPLGKEVIEECAKNYPHVPIIQ | ||||||
Region | 344-407 | SBD2 | ||||
Sequence: GYGLTESCGIASLEIPEGVREYGSSGILFPAVEAKIVHVENLTPLPPNQLGEIWIRGPNMMQGY | ||||||
Motif | 546-548 | Microbody targeting signal | ||||
Sequence: SKI |
Sequence similarities
Belongs to the ATP-dependent AMP-binding enzyme family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length548
- Mass (Da)59,821
- Last updated2020-06-17 v1
- ChecksumF78A25162AC49564