PUN1_CAPAN
ID PUN1_CAPAN Reviewed; 440 AA.
AC D2Y3X2; Q58VS8; Q58VS9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Acyltransferase Pun1 {ECO:0000305};
DE EC=2.3.2.35 {ECO:0000269|PubMed:15918882, ECO:0000269|PubMed:25884984};
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};
GN ORFNames=T459_06020 {ECO:0000312|EMBL:PHT90907.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVE
RP SITE, AND TISSUE SPECIFICITY.
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 [MRNA].
RA Ruan W., Guo Q., Jia C., Guo M.;
RT "Prokaryotic expression of the Pun1 gene for the pungency of pepper.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=31086491; DOI=10.1270/jsbbs.18150;
RA Tsurumaki K., Sasanuma T.;
RT "Discovery of novel unfunctional pAMT allele pamt10 causing loss of
RT pungency in sweet bell pepper (Capsicum annuum L.).";
RL Breed. Sci. 69:133-142(2019).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441736; DOI=10.1038/ng.2877;
RA Kim S., Park M., Yeom S.I., Kim Y.M., Lee J.M., Lee H.A., Seo E., Choi J.,
RA Cheong K., Kim K.T., Jung K., Lee G.W., Oh S.K., Bae C., Kim S.B.,
RA Lee H.Y., Kim S.Y., Kim M.S., Kang B.C., Jo Y.D., Yang H.B., Jeong H.J.,
RA Kang W.H., Kwon J.K., Shin C., Lim J.Y., Park J.H., Huh J.H., Kim J.S.,
RA Kim B.D., Cohen O., Paran I., Suh M.C., Lee S.B., Kim Y.K., Shin Y.,
RA Noh S.J., Park J., Seo Y.S., Kwon S.Y., Kim H.A., Park J.M., Kim H.J.,
RA Choi S.B., Bosland P.W., Reeves G., Jo S.H., Lee B.W., Cho H.T., Choi H.S.,
RA Lee M.S., Yu Y., Do Choi Y., Park B.S., van Deynze A., Ashrafi H., Hill T.,
RA Kim W.T., Pai H.S., Ahn H.K., Yeam I., Giovannoni J.J., Rose J.K.,
RA Soerensen I., Lee S.J., Kim R.W., Choi I.Y., Choi B.S., Lim J.S., Lee Y.H.,
RA Choi D.;
RT "Genome sequence of the hot pepper provides insights into the evolution of
RT pungency in Capsicum species.";
RL Nat. Genet. 46:270-278(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334;
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25884984; DOI=10.1186/s12870-015-0476-7;
RA Ogawa K., Murota K., Shimura H., Furuya M., Togawa Y., Matsumura T.,
RA Masuta C.;
RT "Evidence of capsaicin synthase activity of the Pun1-encoded protein and
RT its role as a determinant of capsaicinoid accumulation in pepper.";
RL BMC Plant Biol. 15:93-93(2015).
RN [7]
RP INDUCTION.
RX PubMed=29372506; DOI=10.1007/s12033-018-0060-0;
RA Kirke J., Kaplan N., Velez S., Jin X.L., Vichyavichien P., Zhang X.H.;
RT "Tissue-preferential activity and induction of the pepper capsaicin
RT synthase PUN1 promoter by wounding, heat and metabolic pathway precursor in
RT tobacco and tomato plants.";
RL Mol. Biotechnol. 60:194-202(2018).
CC -!- FUNCTION: Participates in the biosynthesis of capsaicinoids in pungent
CC cultivars of Capsicum annuum (PubMed:15918882, PubMed:25884984).
CC Capsaicinoids, the alkaloids responsible for the heat or pungency of
CC chili pepper, are synthesized from phenylpropanoid intermediates in the
CC placental tissue of chili peper fruit (Probable). Can transfer an acyl
CC from 8-methylnon-6-enoyl-CoA to vanillylamine forming capsaicin and CoA
CC (PubMed:15918882, PubMed:25884984). {ECO:0000269|PubMed:15918882,
CC ECO:0000269|PubMed:25884984, ECO:0000305}.
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:0000269|PubMed:25884984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63833;
CC Evidence={ECO:0000269|PubMed:25884984};
CC -!- TISSUE SPECIFICITY: Expressed in fruit 20 days post anthesis.
CC {ECO:0000269|PubMed:15918882}.
CC -!- INDUCTION: Induced by wounding and heat. {ECO:0000269|PubMed:29372506}.
CC -!- MISCELLANEOUS: Plants silencing PUN1 exhibit low levels of
CC caspaicinoids in mature fruits compared to wild type plants.
CC {ECO:0000269|PubMed:15918882, ECO:0000269|PubMed:25884984}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AY819028; AAV66310.1; -; Genomic_DNA.
DR EMBL; AY819029; AAV66311.1; -; Genomic_DNA.
DR EMBL; GU300812; ADB28437.1; -; mRNA.
DR EMBL; LC423556; BBG28791.1; -; Genomic_DNA.
DR EMBL; LC423557; BBG28792.1; -; Genomic_DNA.
DR EMBL; AYRZ02000002; PHT90907.1; -; Genomic_DNA.
DR RefSeq; NP_001311698.1; NM_001324769.1.
DR AlphaFoldDB; D2Y3X2; -.
DR SMR; D2Y3X2; -.
DR STRING; 4072.D2Y3X2; -.
DR EnsemblPlants; PHT90907; PHT90907; T459_06020.
DR GeneID; 107859694; -.
DR Gramene; PHT90907; PHT90907; T459_06020.
DR KEGG; cann:107859694; -.
DR OMA; RFPLYKV; -.
DR BioCyc; MetaCyc:MON-13534; -.
DR BioCyc; MetaCyc:MON-21006; -.
DR BRENDA; 2.3.2.35; 1169.
DR Proteomes; UP000189700; Genome assembly.
DR Proteomes; UP000222542; Chromosome 2.
DR GO; GO:0016755; F:aminoacyltransferase activity; IDA:UniProtKB.
DR GO; GO:0009821; P:alkaloid biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..440
FT /note="Acyltransferase Pun1"
FT /id="PRO_0000451975"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15918882"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:15918882"
FT CONFLICT 191
FT /note="R -> H (in Ref. 1; AAV66311/AAV66310)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="L -> F (in Ref. 1; AAV66310)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="L -> V (in Ref. 1; AAV66311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49299 MW; C9F62591BDC665E4 CRC64;
MAFALPSSLV SVCNKSFIKP SSLTPSTLRF HKLSFIDQSL SNMYIPCAFF YPKVQQRLED
SKNSDELSHI AHLLQTSLSQ TLVSYYPYAG KLKDNATVDC NDMGAEFLSV RIKCSMSEIL
DHPHASLAES IVLPKDLPWA NNCEGGNLLV VQVSKFDCGG IAISVCFSHK IGDGCSLLNF
LNDWSSVTRD RTTTTLVPSP RFVGDSVFST QKYGSLITPQ ILSDLNQCVQ KRLIFPTDKL
DALRAKVAEE SGVKNPTRAE VVSALLFKCA TKASSSMLPS KLVHFLNIRT MIKPRLPRNA
IGNLSSIFSI EATNMQDMEL PTLVRNLRKE VEVAYKKDQV EQNELILEVV ESMREGKLPF
ENMDGYKNVY TCSNLCKYPY YTVDFGWGRP ERVCLGNGPS KNAFFLKDYK AGQGVEARVM
LHKQQMSEFE RNEELLEFIA
