ID   HHT1_AVESA              Reviewed;         441 AA.
AC   Q7XXP3;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Hydroxycinnamoyl-CoA:5-hydroxyanthranilate N-hydroxycinnamoyltransferase HHT1 {ECO:0000305};
DE            EC=2.3.1.302 {ECO:0000269|PubMed:31394723};
DE   AltName: Full=Hydroxyanthranilate hydroxycinnamoyltransferase 1 {ECO:0000303|PubMed:14714871};
DE            Short=AsHHT1 {ECO:0000303|PubMed:14714871};
GN   Name=HHT1 {ECO:0000303|PubMed:14714871};
OS   Avena sativa (Oat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Aveninae; Avena.
OX   NCBI_TaxID=4498;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   PubMed=14714871; DOI=10.1094/mpmi.2004.17.1.81;
RA   Yang Q., Trinh H.X., Imai S., Ishihara A., Zhang L., Nakayashiki H.,
RA   Tosa Y., Mayama S.;
RT   "Analysis of the involvement of hydroxyanthranilate
RT   hydroxycinnamoyltransferase and caffeoyl-CoA 3-O-methyltransferase in
RT   phytoalexin biosynthesis in oat.";
RL   Mol. Plant Microbe Interact. 17:81-89(2004).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31394723; DOI=10.3390/metabo9080163;
RA   Li Z., Chen Y., Meesapyodsuk D., Qiu X.;
RT   "The biosynthetic pathway of major avenanthramides in oat.";
RL   Metabolites 9:0-0(2019).
CC   -!- FUNCTION: Involved in the biosynthesis of avenanthramide phytoalexins,
CC       which are phenolic alkaloids found mainly in oats (PubMed:31394723).
CC       Catalyzes the N-acylation of 5-hydroxyanthranilate with 4-coumaroyl-CoA
CC       or caffeoyl-CoA as acyl donors, forming avenanthramide A and
CC       avenanthramide C, respectively (PubMed:31394723). Does not accept
CC       feruloyl-CoA as a substrate (PubMed:31394723).
CC       {ECO:0000269|PubMed:31394723}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumaroyl-CoA + 5-hydroxyanthranilate = avenanthramide A
CC         + CoA; Xref=Rhea:RHEA:66932, ChEBI:CHEBI:57287, ChEBI:CHEBI:85008,
CC         ChEBI:CHEBI:167463, ChEBI:CHEBI:167464; EC=2.3.1.302;
CC         Evidence={ECO:0000269|PubMed:31394723};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66933;
CC         Evidence={ECO:0000269|PubMed:31394723};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeoyl-CoA + 5-hydroxyanthranilate = avenanthramide C +
CC         CoA; Xref=Rhea:RHEA:66936, ChEBI:CHEBI:57287, ChEBI:CHEBI:87136,
CC         ChEBI:CHEBI:167463, ChEBI:CHEBI:167577; EC=2.3.1.302;
CC         Evidence={ECO:0000269|PubMed:31394723};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66937;
CC         Evidence={ECO:0000269|PubMed:31394723};
CC   -!- INDUCTION: Induced by the crown rust fungus Puccinia coronata and the
CC       phytotoxin victorin. {ECO:0000269|PubMed:14714871}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; AB076980; BAC78633.1; -; mRNA.
DR   SMR; Q7XXP3; -.
DR   KEGG; ag:BAC78633; -.
DR   BRENDA; 2.3.1.302; 588.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:UniProt.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Plant defense; Transferase.
FT   CHAIN           1..441
FT                   /note="Hydroxycinnamoyl-CoA:5-hydroxyanthranilate N-
FT                   hydroxycinnamoyltransferase HHT1"
FT                   /id="PRO_0000454971"
FT   ACT_SITE        158
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT   ACT_SITE        388
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
SQ   SEQUENCE   441 AA;  47918 MW;  F8C3412BB5B97B74 CRC64;
     MKITVRSSTV VVPAAETPRV RLWNANPDLV VPRFHTPSVY FYRRGGEDGG DACYFDAGRM
     RRALAEALVP FYPMAGRLAH DEDGRVEIDC NAEGVLFVEA DAPDGAVDDF GDFVPTMGLK
     RLIPTVDFTG GISSYPLLVV QVTHFKCGGV ALGIAMQHHV ADGFSGLHFI NSWSDLCRGV
     PIAVMPFIDR TLLRARDPPV PTHPHIEYQP APAMLGSEEP QALAGKPESP PTAVDIFKLS
     RSDLGRLRAQ LPTGEGAPRF STYAVLGAHV WRCASLARGL APEQPTKLYC ATDGRQRLTP
     THPDGYFGNV IFTATPLAEA GKVTGSLADG ATTIQDALEK MDDEYCHSAL DYLELQPDLS
     ALVRGAHTFR CPNLGLTSWV RLPIHDADFG WGRPVFMGPG GIAYEGLAFV LPSANRDGSL
     SVAISLQAEH MEKFRKMIFD F