ID   THT11_TOBAC             Reviewed;         226 AA.
AC   Q9SMB8; Q9SMB9;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Tyramine N-feruloyltransferase 4/11;
DE            EC=2.3.1.110;
DE   AltName: Full=Hydroxycinnamoyl-CoA: tyramine N-hydroxycinnamoyltransferase;
GN   Name=THT4;
GN   and
GN   Name=THT11;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (THT4 AND THT11).
RC   STRAIN=cv. Bottom Special; TISSUE=Leaf;
RX   PubMed=10469131; DOI=10.1046/j.1432-1327.1999.00538.x;
RA   Farmer M.J., Czernic P., Michael A., Negrel J.;
RT   "Identification and characterization of cDNA clones encoding
RT   hydroxycinnamoyl-CoA:tyramine N-hydroxycinnamoyltransferase from tobacco.";
RL   Eur. J. Biochem. 263:686-694(1999).
CC   -!- FUNCTION: Synthesizes amides which are involved in stress response in
CC       the cell wall. Catalyzes the synthesis of hydroxycinnamic acid amides
CC       from hydroxycinnamoyl-CoA thioesters and various
CC       hydroxyphenylethylamines such as 4-coumaroyl-CoA and sinapoyl-CoA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-feruloyl-CoA + tyramine = CoA + H(+) + N-[(E)-
CC         feruloyl]tyramine; Xref=Rhea:RHEA:19685, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17818, ChEBI:CHEBI:57287, ChEBI:CHEBI:87305,
CC         ChEBI:CHEBI:327995; EC=2.3.1.110;
CC   -!- ACTIVITY REGULATION: Inhibited by (2-hydroxyphenyl)amino sulfinyl
CC       acetic acid 1,1-dimethylethyl ester, by DEPC and by N-ethylmaleimide.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB55501.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ131767; CAB55501.1; ALT_INIT; mRNA.
DR   EMBL; AJ131768; CAB55502.1; -; mRNA.
DR   RefSeq; NP_001313019.1; NM_001326090.1.
DR   AlphaFoldDB; Q9SMB8; -.
DR   SMR; Q9SMB8; -.
DR   GeneID; 107822189; -.
DR   KEGG; nta:107822189; -.
DR   OMA; ENDIHHI; -.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central.
DR   GO; GO:0050366; F:tyramine N-feruloyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR032960; Tyra_N_feruloTrfase.
DR   PANTHER; PTHR10545:SF54; PTHR10545:SF54; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..226
FT                   /note="Tyramine N-feruloyltransferase 4/11"
FT                   /id="PRO_0000074602"
FT   DOMAIN          72..222
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   REGION          29..45
FT                   /note="Important in binding site and for catalytic
FT                   activity"
FT                   /evidence="ECO:0000255"
FT   SITE            157
FT                   /note="Important for catalytic activity"
FT   SITE            160
FT                   /note="Important for catalytic activity"
FT   SITE            162
FT                   /note="Important for catalytic activity"
SQ   SEQUENCE   226 AA;  25977 MW;  63F92D02058A0487 CRC64;
     MATTNNKNLT ITEKVYVRVR LANEADISHI YKLFYQIHEY HNYTHLYKAT ESSLCDLLFK
     ANPNPLFYGP SVLLLEVSPT PFENTKKDEK FKPVLKTFDL RATVEDKEAE EFKSKSCGDE
     KEDVFIAGYA FFYANYSCFY DKAGIYFESL YFRESYRKLG MGSLLFGTVA SIAANNGFAS
     VEGIVAVWNK KSYDFYVNMG VEIFDEFRYG KLVGDALQKY ADKEKA