ID   HHT4_AVESA              Reviewed;         445 AA.
AC   A0A4Y5UJ70;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   03-AUG-2022, entry version 9.
DE   RecName: Full=Hydroxycinnamoyl-CoA:5-hydroxyanthranilate N-hydroxycinnamoyltransferase HHT4 {ECO:0000305};
DE            EC=2.3.1.302 {ECO:0000269|PubMed:31394723};
DE   AltName: Full=Hydroxyanthranilate hydroxycinnamoyltransferase 4 {ECO:0000303|PubMed:14714871};
DE            Short=AsHHT4 {ECO:0000303|PubMed:14714871};
GN   Name=HHT4 {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], 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).
RN   [2]
RP   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).
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.
CC       {ECO:0000269|PubMed:14714871}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; MH397064; QDC27803.1; -; mRNA.
DR   KEGG; ag:QDC27803; -.
DR   BioCyc; MetaCyc:MON-21254; -.
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..445
FT                   /note="Hydroxycinnamoyl-CoA:5-hydroxyanthranilate N-
FT                   hydroxycinnamoyltransferase HHT4"
FT                   /id="PRO_0000454972"
SQ   SEQUENCE   445 AA;  48217 MW;  0BF888C372BEA95C CRC64;
     MAITVRRSTM VRPAAERPRE RLWNSNLDLV VPRFHTPSVY FYRRPDAGAG AGPGAAEGFF
     DAERMRRALA EALVPFYPMA GRLARDEDGR VEIDCSGEGV LFVEARAPGA AVDDYGDFAP
     TMELKRLIPA VDYSGDISSF PLLVLQVTYF KCGGVSLGVG MQHHVADGMS GLHFINSWSD
     LCRGAQIAVM PFIDRTLLRA RDPPTPSYTH VEYQPAPAML SSAPQALTGK PTLAPTAVDI
     FKLTRSELGR LRAQLPTGEG APRFSTYAVL AAHVWRCVSL ARGLPAEQPT KLYCATDGRH
     RLQPPLPEGY FGNVIFTATP LAEAGKVTGA VADGAAVIQG ALDRMSDDYC RSALDYLETQ
     PDLSALVRGA HTFRCPNLGL TSWVRLPIHD ADFGWGRPVF MGPGGIAYEG LAFVLPSANK
     DGSLSIAISL QAEHMEKFRK LIADV