AGCT1_HORVU
ID AGCT1_HORVU Reviewed; 439 AA.
AC A9ZPJ6; Q84QG6;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Agmatine coumaroyltransferase-1 {ECO:0000303|PubMed:18270436, ECO:0000312|EMBL:BAF97626.1};
DE EC=2.3.1.64;
GN Name=ACT-1; Synonyms=ACT {ECO:0000312|EMBL:AAO73071.1};
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:0000305, ECO:0000312|EMBL:AAO73071.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-15, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=cv. Triumph {ECO:0000269|PubMed:12582168};
RC TISSUE=Leaf {ECO:0000312|EMBL:AAO73071.1};
RX PubMed=12582168; DOI=10.1074/jbc.m213041200;
RA Burhenne K., Kristensen B.K., Rasmussen S.K.;
RT "A new class of N-hydroxycinnamoyltransferases. Purification, cloning, and
RT expression of a barley agmatine coumaroyltransferase (EC 2.3.1.64).";
RL J. Biol. Chem. 278:13919-13927(2003).
RN [2] {ECO:0000312|EMBL:BAF97626.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Betzes {ECO:0000269|PubMed:18270436};
RC TISSUE=Shoot {ECO:0000312|EMBL:BAF97626.1};
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 [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=cv. Proctor {ECO:0000269|Ref.3};
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.
CC {ECO:0000269|PubMed:12582168, ECO:0000269|Ref.3}.
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|PubMed:12582168, ECO:0000269|Ref.3};
CC -!- ACTIVITY REGULATION: Inhibited by DEPC. Completely inhibited by
CC ZnSO(4), strongly inhibited by CuSO(4), partially inhibited by MnCl(2).
CC Unaffected by MgCl(2) or CaCl(2). {ECO:0000269|PubMed:12582168}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.1 uM for agmatine {ECO:0000269|PubMed:12582168,
CC ECO:0000269|Ref.3};
CC KM=2.1 uM for 4-coumaroyl-CoA {ECO:0000269|PubMed:12582168,
CC ECO:0000269|Ref.3};
CC KM=6.6 uM for feruloyl-CoA {ECO:0000269|PubMed:12582168,
CC ECO:0000269|Ref.3};
CC KM=4.3 uM for caffeoyl-CoA {ECO:0000269|PubMed:12582168,
CC ECO:0000269|Ref.3};
CC pH dependence:
CC Optimum pH is 7.5. Half maximum activity is seen at pH 6.9 and 8.1.
CC {ECO:0000269|PubMed:12582168, ECO:0000269|Ref.3};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:12582168, ECO:0000269|Ref.3};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12582168}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY228552; AAO73071.1; -; mRNA.
DR EMBL; AB334132; BAF97626.1; -; mRNA.
DR PDB; 7CYS; X-ray; 1.81 A; A=2-439.
DR PDBsum; 7CYS; -.
DR AlphaFoldDB; A9ZPJ6; -.
DR SMR; A9ZPJ6; -.
DR BioCyc; MetaCyc:MON-15451; -.
DR BRENDA; 2.3.1.64; 2687.
DR ExpressionAtlas; A9ZPJ6; baseline.
DR GO; GO:0047634; F:agmatine N4-coumaroyltransferase activity; IDA:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Direct protein sequencing; Transferase.
FT CHAIN 1..439
FT /note="Agmatine coumaroyltransferase-1"
FT /id="PRO_0000405023"
FT ACT_SITE 152
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT VARIANT 208
FT /note="C -> Y (in strain: cv. Triumph)"
FT /evidence="ECO:0000269|PubMed:12582168"
FT VARIANT 243
FT /note="H -> Q (in strain: cv. Triumph)"
FT /evidence="ECO:0000269|PubMed:12582168"
FT VARIANT 378
FT /note="R -> L (in strain: cv. Triumph)"
FT /evidence="ECO:0000269|PubMed:12582168"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7CYS"
FT TURN 33..37
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 41..49
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 131..138
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:7CYS"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 157..172
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:7CYS"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 225..232
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 234..245
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 254..270
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:7CYS"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 312..317
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 320..333
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 336..346
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 356..359
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 371..375
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:7CYS"
FT STRAND 417..424
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:7CYS"
FT HELIX 428..435
FT /evidence="ECO:0007829|PDB:7CYS"
SQ SEQUENCE 439 AA; 47467 MW; 50BA34E028FF8DD7 CRC64;
MKITVHSSKA VKPEYGACGL APGCTADVVP LTVLDKANFD TYISVIYAFH APAPPNAVLE
AGLGRALVDY REWAGRLGVD ASGGRAILLN DAGARFVEAT ADVALDSVMP LKPTSEVLSL
HPSGDDGPEE LMLIQVTRFA CGSLVVGFTT QHIVSDGRST GNFFVAWSQA TRGAAIDPVP
VHDRASFFHP REPLHVEYEH RGVEFKPCEK AHDVVCGADG DEDEVVVNKV HFSREFISKL
KAHASAGAPR PCSTLQCVVA HLWRSMTMAR GLDGGETTSV AIAVDGRARM SPQVPDGYTG
NVILWARPTT TAGELVTRPV KHAVELISRE VARINDGYFK SFIDFANSGA VEKERLVATA
DAADMVLSPN IEVDSWLRIP FYDMDFGGGR PFFFMPSYLP VEGLLILLPS FLGDGSVDAY
VPLFSRDMNT FKNCCYSLD
