ID   3AT_PERFR               Reviewed;         446 AA.
AC   Q9MBC1;
DT   29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Anthocyanidin 3-O-glucoside 6''-O-acyltransferase;
DE            Short=3AT;
DE            EC=2.3.1.215;
DE   Flags: Fragment;
OS   Perilla frutescens (Beefsteak mint) (Perilla ocymoides).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Elsholtzieae; Perilla.
OX   NCBI_TaxID=48386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Leaf;
RX   PubMed=10845463; DOI=10.1093/pcp/41.4.495;
RA   Yonekura-Sakakibara K., Tanaka Y., Fukuchi-Mizutani M., Fujiwara H.,
RA   Fukui Y., Ashikari T., Murakami Y., Yamaguchi M., Kusumi T.;
RT   "Molecular and biochemical characterization of a novel hydroxycinnamoyl-
RT   CoA: anthocyanin 3-O-glucoside-6'-O-acyltransferase from Perilla
RT   frutescens.";
RL   Plant Cell Physiol. 41:495-502(2000).
RN   [2]
RP   IDENTIFICATION.
RA   Fujiwara H., Tanaka Y., Fukui Y., Ashikari T., Yamaguchi M., Kusumi T.;
RT   "Purification and characterization of anthocyanin 3-aromatic
RT   acyltransferase from Perilla frutescens.";
RL   Plant Sci. 137:87-94(1998).
CC   -!- FUNCTION: Catalyzes the transfer of the p-coumaric and caffeic acids
CC       from their CoA esters to the 3-glucosyl moiety of a range of
CC       anthocyanidin 3-O-glucosides, 3,5-di-O-glucosides and cyanidin 3-
CC       rutinoside. Anthocyanins are ubiquitous colored pigments that are
CC       responsible for petal color. Does not act on delphinidin 3,3',7-tri-O-
CC       glucoside. Recombinant enzyme can use caffeoyl-CoA but not malonyl-CoA
CC       as alternative acyl donor. {ECO:0000269|PubMed:10845463}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumaroyl-CoA + an anthocyanidin 3-O-beta-D-glucoside =
CC         an anthocyanidin 3-O-[6-O-(4-hydroxycinnamoyl)-beta-D-glucoside] +
CC         CoA + H(+); Xref=Rhea:RHEA:35411, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16307, ChEBI:CHEBI:57287, ChEBI:CHEBI:71505,
CC         ChEBI:CHEBI:85008; EC=2.3.1.215;
CC         Evidence={ECO:0000269|PubMed:10845463};
CC   -!- PATHWAY: Pigment biosynthesis; anthocyanin biosynthesis.
CC       {ECO:0000269|PubMed:10845463}.
CC   -!- TISSUE SPECIFICITY: Detected in the young leaves of perilla red forma.
CC       {ECO:0000269|PubMed:10845463}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; AB029340; BAA93475.1; -; mRNA.
DR   AlphaFoldDB; Q9MBC1; -.
DR   SMR; Q9MBC1; -.
DR   KEGG; ag:BAA93475; -.
DR   BioCyc; MetaCyc:MON-12110; -.
DR   BRENDA; 2.3.1.215; 4681.
DR   UniPathway; UPA00009; -.
DR   GO; GO:0102453; F:anthocyanidin 3-O-glucoside 6''-O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009718; P:anthocyanin-containing compound biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Transferase.
FT   CHAIN           <1..446
FT                   /note="Anthocyanidin 3-O-glucoside 6''-O-acyltransferase"
FT                   /id="PRO_0000422580"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        389
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   446 AA;  50675 MW;  DC83C69AF248A593 CRC64;
     VIETCRVGPP PDSVAEQSVP LTFFDMTWLH FHPMLQLLFY EFPCSKQHFS ESIVPKLKQS
     LSKTLIHFFP LSCNLIYPSS PEKMPEFRYL SGDSVSFTIA ESSDDFDDLV GNRPESPVRL
     YNFVPKLPPI VEESDRKLFQ VFAVQVTLFP GRGVGIGIAT HHTVSDAPSF LAFITAWSSM
     SKHIENEDED EEFKSLPVFD RSVIKYPTKF DSIYWRNALK FPLQSRHPSL PTDRIRTTFV
     FTQSKIKKLK GWIQSRVPSL VHLSSFVAIA AYMWAGITKS FTADEDQDNE DAFFLIPVDL
     RPRLDPPVPE NYFGNCLSYA LPRMRRRELV GEKGVFLAAE VIAAEIKKRI NDKRILETVE
     KWSPEIRKAL QKSYFSVAGS SKLDLYGADF GWGKARKQEI LSIDGEKYAM TLCKARDFEG
     GLEVCLSLPK DKMDAFAAYF SLGING