ID   AGCT2_HORVU             Reviewed;         439 AA.
AC   A9ZPJ7;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Agmatine coumaroyltransferase-2 {ECO:0000303|PubMed:18270436, ECO:0000312|EMBL:BAF97627.1};
DE            EC=2.3.1.64;
GN   Name=ACT-2;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1] {ECO:0000312|EMBL:BAF97627.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Betzes {ECO:0000269|PubMed:18270436};
RC   TISSUE=Shoot {ECO:0000312|EMBL:BAF97627.1};
RX   PubMed=18270436; DOI=10.1266/ggs.82.455;
RA   Nomura T., Ishizuka A., Kishida K., Islam A.K.M.R., Endo T.R., Iwamura H.,
RA   Ishihara A.;
RT   "Chromosome arm location of the genes for the biosynthesis of hordatines in
RT   barley.";
RL   Genes Genet. Syst. 82:455-464(2007).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=cv. Proctor {ECO:0000269|Ref.2};
RA   Bird C.R., Smith T.A.;
RT   "Agmatine coumaroyltransferase from barley seedlings.";
RL   Phytochemistry 22:2401-2403(1983).
CC   -!- FUNCTION: Involved in the synthesis of hordatines (antifungal
CC       hydroxycinnamoylagmatine derivatives). Specific for agmatine as the
CC       acyl acceptor, inactive towards tyramine and putrescine. Has activity
CC       with the acyl donors 4-coumaroyl-CoA, cinnamoyl-CoA, caffeoyl-CoA,
CC       feruloyl-CoA, and to a lesser extent sinapoyl-CoA. {ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-coumaroyl-CoA + agmatine = CoA + H(+) + N-(4-
CC         guanidinobutyl)-4-hydroxycinnamamide; Xref=Rhea:RHEA:13405,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57355,
CC         ChEBI:CHEBI:58145, ChEBI:CHEBI:58644; EC=2.3.1.64;
CC         Evidence={ECO:0000269|Ref.2};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|Ref.2};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A9ZPJ6}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000255}.
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DR   EMBL; AB334133; BAF97627.1; -; mRNA.
DR   AlphaFoldDB; A9ZPJ7; -.
DR   SMR; A9ZPJ7; -.
DR   ExpressionAtlas; A9ZPJ7; baseline.
DR   GO; GO:0047634; F:agmatine N4-coumaroyltransferase activity; ISS:UniProtKB.
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..439
FT                   /note="Agmatine coumaroyltransferase-2"
FT                   /id="PRO_0000405024"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        385
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   439 AA;  47641 MW;  9D4620315DA3886A CRC64;
     MKITVHSSKA VKPEYGACGV APGCTADVVP LTVLDKANFD TYISVIYAFH PPAPPNAVLE
     AGLGRALVDY REWAGRLGVD ANGDRAILLN DAGARFVEAT ADVALDSVMP LKPTSEVLSL
     HPSGDDGPEE LMLIQVTRFA CGSLVVGFTA QHLVSDGRAT SNFFLAWSQA TRGVAVDPVP
     VHDRASFFHP REPLHVEYEH RGVEFKPYEK AHDVVCGADG DEDEVVVNKV HFSREFISKL
     KAQASAGAPR PCSTLQCVVA HLWRSMTMAR GLDGGETTSV AIAVDGRARM SPQVPDGYTG
     NVILWARPTT TAGELVDRPV KHAVELISRE VARINDGYFK SFIDFANSGA VEKERLVATA
     DAADMVLSPN IEVDSWLRIP FYDMDFGGGR PFFFMPSYLP VEGLLILLPS FLGDGSVDAY
     VPLFSRDMNT FKNCCYSLD