AGCT_ARATH
ID AGCT_ARATH Reviewed; 452 AA.
AC Q9FNP9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Agmatine coumaroyltransferase {ECO:0000303|PubMed:19521717};
DE EC=2.3.1.64;
GN Name=ACT {ECO:0000303|PubMed:19521717}; OrderedLocusNames=At5g61160;
GN ORFNames=MAF19.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAK59784.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:14593172};
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4] {ECO:0000305}
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia {ECO:0000269|PubMed:19521717};
RX PubMed=19521717; DOI=10.1007/s00425-009-0960-0;
RA Muroi A., Ishihara A., Tanaka C., Ishizuka A., Takabayashi J., Miyoshi H.,
RA Nishioka T.;
RT "Accumulation of hydroxycinnamic acid amides induced by pathogen infection
RT and identification of agmatine coumaroyltransferase in Arabidopsis
RT thaliana.";
RL Planta 230:517-527(2009).
CC -!- FUNCTION: Involved in the biosynthesis of hydroxycinnamic acid amides,
CC which play a role in defense against pathogens. Agmatine is the
CC preferred acyl acceptor, lower activity is observed towards putrescine.
CC The preferred acyl donor is p-coumaroyl-CoA, lower activity is seen
CC towards feruloyl-CoA. {ECO:0000269|PubMed:19521717}.
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:19521717};
CC -!- DISRUPTION PHENOTYPE: Increased susceptibility to A.brassicicola
CC infection. {ECO:0000269|PubMed:19521717}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000255}.
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DR EMBL; AB006696; BAB10378.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97429.1; -; Genomic_DNA.
DR EMBL; AY037199; AAK59784.1; -; mRNA.
DR EMBL; AY133543; AAM91373.1; -; mRNA.
DR RefSeq; NP_200924.1; NM_125509.3.
DR AlphaFoldDB; Q9FNP9; -.
DR SMR; Q9FNP9; -.
DR STRING; 3702.AT5G61160.1; -.
DR PaxDb; Q9FNP9; -.
DR PRIDE; Q9FNP9; -.
DR ProteomicsDB; 244739; -.
DR DNASU; 836237; -.
DR EnsemblPlants; AT5G61160.1; AT5G61160.1; AT5G61160.
DR GeneID; 836237; -.
DR Gramene; AT5G61160.1; AT5G61160.1; AT5G61160.
DR KEGG; ath:AT5G61160; -.
DR Araport; AT5G61160; -.
DR TAIR; locus:2159476; AT5G61160.
DR eggNOG; ENOG502QPXT; Eukaryota.
DR HOGENOM; CLU_014546_7_0_1; -.
DR InParanoid; Q9FNP9; -.
DR OMA; GWRERIV; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9FNP9; -.
DR BioCyc; ARA:AT5G61160-MON; -.
DR BRENDA; 2.3.1.64; 399.
DR PRO; PR:Q9FNP9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNP9; baseline and differential.
DR Genevisible; Q9FNP9; AT.
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 Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..452
FT /note="Agmatine coumaroyltransferase"
FT /id="PRO_0000405009"
FT ACT_SITE 163
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 396
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 452 AA; 51075 MW; 0FA5A87D0BA22869 CRC64;
MALKVIKISR VSPATASVDP LIVPLSFFDL QWLKLNPTEQ VFFYKLTESS SSRDVFYSSI
LPKLERSLSL ILTHFRLFTG HLKWDSQDPK PHLVVLSGDT LSLTVAETDA DFSRISGRGL
RPELELRPLI PELPIYSDSG AVVSLQVTLF PKQGFCIGTT AHHVVLDGKT AEKFNKAWAH
TCKHGTIPKI LPTVLDRSVV NVPAGLEQKM LELLPYLTED DKENGRTLKL PPVKEINAKD
NVLRITIEIS PENIEKLKER AKKESTRAEL HLSTFVVTFA HVWTCMVKAR SGDPNRPVRF
MYAADFRNRL EPPVPVTYFG TCVLAMDFYK YKAKEFMGED GFVNTVEILS DSVKRLASQG
VESTWKVYEE GTKTMKWGTQ LLVVNGSNQI GMYETDFGWG RPIHTETMSI YKNDEFSMSK
RRDGIGGVEI GISLKKLEMD TFLSLFYKWI GN
