PUN1_CAPFR
ID PUN1_CAPFR Reviewed; 440 AA.
AC Q58VT1; E2J5K6;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Acyltransferase Pun1 {ECO:0000305};
DE EC=2.3.2.35 {ECO:0000250|UniProtKB:D2Y3X2};
DE AltName: Full=Acyltransferase 3 {ECO:0000303|PubMed:15918882};
DE AltName: Full=Capsaicin synthase {ECO:0000305};
DE AltName: Full=Protein PUNGENT 1 {ECO:0000303|PubMed:15918882};
GN Name=PUN1 {ECO:0000303|PubMed:15918882};
GN Synonyms=AT3 {ECO:0000303|PubMed:15918882};
OS Capsicum frutescens (Cayenne pepper) (Tabasco pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4073;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15918882; DOI=10.1111/j.1365-313x.2005.02410.x;
RA Stewart C., Kang B.C., Liu K., Mazourek M., Moore S.L., Yoo E.Y., Kim B.D.,
RA Paran I., Jahn M.M.;
RT "The Pun1 gene for pungency in pepper encodes a putative acyltransferase.";
RL Plant J. 42:675-688(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Deng M.H., Wen J.F., Zou X.X., Zhu H.S.;
RT "Clone and sequence analysis of acyltransferase (Pun1) gene in pepper.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the biosynthesis of capsaicinoids in pungent
CC cultivars of Capsicum frutescens. Capsaicinoids, the alkaloids
CC responsible for the heat or pungency of chili pepper, are synthesized
CC from phenylpropanoid intermediates in the placental tissue of chili
CC peper fruit. Can transfer an acyl from 8-methylnon-6-enoyl-CoA to
CC vanillylamine forming capsaicin and CoA.
CC {ECO:0000250|UniProtKB:D2Y3X2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(6E)-8-methylnon-6-enoyl-CoA + vanillylamine = capsaicin + CoA
CC + H(+); Xref=Rhea:RHEA:63832, ChEBI:CHEBI:3374, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:149596, ChEBI:CHEBI:149597;
CC EC=2.3.2.35; Evidence={ECO:0000250|UniProtKB:D2Y3X2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63833;
CC Evidence={ECO:0000250|UniProtKB:D2Y3X2};
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY819026; AAV66308.1; -; Genomic_DNA.
DR EMBL; HM854860; ADN97116.1; -; Genomic_DNA.
DR AlphaFoldDB; Q58VT1; -.
DR SMR; Q58VT1; -.
DR GO; GO:0016755; F:aminoacyltransferase activity; ISS:UniProtKB.
DR GO; GO:0009821; P:alkaloid biosynthetic process; ISS:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 3: Inferred from homology;
KW Acyltransferase; Transferase.
FT CHAIN 1..440
FT /note="Acyltransferase Pun1"
FT /id="PRO_0000451977"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:D2Y3X2"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:D2Y3X2"
FT CONFLICT 12
FT /note="I -> V (in Ref. 2; ADN97116)"
FT /evidence="ECO:0000305"
FT CONFLICT 27
FT /note="T -> K (in Ref. 2; ADN97116)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="T -> A (in Ref. 2; ADN97116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49297 MW; 4669F6861ED6070E CRC64;
MAFALPSSLV SICDKSFIKP SSLTPSTLRF HKLSFIDQSL SNMYIPCAFF YPKVQQRLED
SKNSDELSHI AHLLQTSLSQ TLVSYYPYAG KLKDNATVDC NDMGAEFLSV RIKCSMSEIL
DHPHASLAES IVLPKDLPWA NNCEGGNLLV VQVSKFDCGG IAISVCFSHK IGDGCSLLNF
LNDWSSVTRD HTTTTLVPSP RFVGDSVFST KKYGSLITPQ ILSDLNECVQ KRLIFPTDKL
DALRAKVAEE SGVKNPTRAE VVSALLFKCA TKASSSMLPS KLVHFLNIRT MIKPRLPRNA
IGNLSSIFSI EATNMQDMEL PTLVRNLRKE VEVAYKKDQV EQNELILEVV ESMREGKLPF
ENMDGYENVY TCSNLCKYPY YTVDFGWGRP ERVCLGNGPS KNAFFLKDYK AGQGVEARVM
LHKQQMSEFE RNEELLEFIA