ID   ANTA_GENTR              Reviewed;         469 AA.
AC   Q9ZWR8;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Anthocyanin 5-aromatic acyltransferase;
DE            Short=5AT;
DE            EC=2.3.1.153;
OS   Gentiana triflora (Clustered gentian).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Gentianaceae; Gentianeae; Gentianinae;
OC   Gentiana.
OX   NCBI_TaxID=55190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 68-89; 249-262; 395-404 AND
RP   442-459, CHARACTERIZATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Petal;
RX   PubMed=9881162; DOI=10.1046/j.1365-313x.1998.00312.x;
RA   Fujiwara H., Tanaka Y., Yonekura-Sakakibara K., Fukuchi-Mizutani M.,
RA   Nakao M., Fukui Y., Yamaguchi M., Ashikari T., Kusumi T.;
RT   "cDNA cloning, gene expression and subcellular localization of anthocyanin
RT   5-aromatic acyltransferase from Gentiana triflora.";
RL   Plant J. 16:421-431(1998).
CC   -!- FUNCTION: Transfers hydroxycinnamic moieties to the glucosyl groups of
CC       anthocyanin.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-4-coumaroyl-CoA + an anthocyanidin 3,5-di-O-beta-D-
CC         glucoside = an anthocyanidin 3-O-beta-D-glucoside 5-O-beta-D-[(6-O-
CC         (E)-4-coumaroyl)glucoside] + CoA; Xref=Rhea:RHEA:15661,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57503, ChEBI:CHEBI:85008,
CC         ChEBI:CHEBI:144773; EC=2.3.1.153;
CC   -!- ACTIVITY REGULATION: Activity enhanced by manganese ions and inhibited
CC       by p-chloromercuribenzoate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9881162}.
CC   -!- TISSUE SPECIFICITY: Expressed in the outer epidermal cells of petals,
CC       but not in sepals, leaves or stems. {ECO:0000269|PubMed:9881162}.
CC   -!- DEVELOPMENTAL STAGE: Induced during petal development and then
CC       decreases rapidly with maturation of the flower.
CC       {ECO:0000269|PubMed:9881162}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: Cannot use malonyl-CoA as a donor.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; AB010708; BAA74428.1; -; mRNA.
DR   PDB; 7DEV; X-ray; 3.10 A; A=1-469.
DR   PDB; 7DEX; X-ray; 2.50 A; A=1-465.
DR   PDBsum; 7DEV; -.
DR   PDBsum; 7DEX; -.
DR   AlphaFoldDB; Q9ZWR8; -.
DR   SMR; Q9ZWR8; -.
DR   KEGG; ag:BAA74428; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047183; F:anthocyanin 5-aromatic acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102815; F:caffeoyl-CoA:delphinidin-3,5-diglucoside 5-O-glucoside-6-O-hydroxycinnamoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102777; F:caffeoyl-CoA:pelargonidin-3,5-diglucoside 5-O-glucoside-6-O-hydroxycinnamoyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW   Transferase.
FT   CHAIN           1..469
FT                   /note="Anthocyanin 5-aromatic acyltransferase"
FT                   /id="PRO_0000147362"
FT   ACT_SITE        174
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        411
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   STRAND          7..15
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          19..22
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   TURN            32..34
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          43..50
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           55..60
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           62..74
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           78..81
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          82..89
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           100..102
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          106..113
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           117..120
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           128..132
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          142..144
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          146..152
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          154..161
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          165..172
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   TURN            174..176
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           179..195
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   TURN            201..205
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           221..235
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          249..255
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           257..271
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           281..299
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   TURN            305..307
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          311..320
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          338..346
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           347..351
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           355..370
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           377..383
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           384..387
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           393..395
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          396..400
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           407..409
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          412..414
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          418..421
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           423..427
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          430..435
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          437..439
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   STRAND          443..449
FT                   /evidence="ECO:0007829|PDB:7DEX"
FT   HELIX           451..462
FT                   /evidence="ECO:0007829|PDB:7DEX"
SQ   SEQUENCE   469 AA;  52740 MW;  EDFFB0B5E5963ACE CRC64;
     MEQIQMVKVL EKCQVTPPSD TTDVELSLPV TFFDIPWLHL NKMQSLLFYD FPYPRTHFLD
     TVIPNLKASL SLTLKHYVPL SGNLLMPIKS GEMPKFQYSR DEGDSITLIV AESDQDFDYL
     KGHQLVDSND LHGLFYVMPR VIRTMQDYKV IPLVAVQVTV FPNRGIAVAL TAHHSIADAK
     SFVMFINAWA YINKFGKDAD LLSANLLPSF DRSIIKDLYG LEETFWNEMQ DVLEMFSRFG
     SKPPRFNKVR ATYVLSLAEI QKLKNKVLNL RGSEPTIRVT TFTMTCGYVW TCMVKSKDDV
     VSEESSNDEN ELEYFSFTAD CRGLLTPPCP PNYFGNCLAS CVAKATHKEL VGDKGLLVAV
     AAIGEAIEKR LHNEKGVLAD AKTWLSESNG IPSKRFLGIT GSPKFDSYGV DFGWGKPAKF
     DITSVDYAEL IYVIQSRDFE KGVEIGVSLP KIHMDAFAKI FEEGFCSLS