ID   THT2_ORYSJ              Reviewed;         434 AA.
AC   Q8LMI4; Q0IY16;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Tryptamine hydroxycinnamoyltransferase 2 {ECO:0000305};
DE            Short=OsTHT2 {ECO:0000303|PubMed:27354554};
DE            EC=2.3.1.- {ECO:0000305};
GN   Name=THT2 {ECO:0000303|PubMed:27354554};
GN   OrderedLocusNames=Os10g0380100 {ECO:0000312|EMBL:BAT10622.1},
GN   LOC_Os10g23820 {ECO:0000312|EMBL:AAP53439.1};
GN   ORFNames=OSJNBa0032N04.1 {ECO:0000312|EMBL:AAM74310.1};
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12791992; DOI=10.1126/science.1083523;
RA   Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA   Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA   Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA   Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA   Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA   Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA   Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA   Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA   Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA   Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA   Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA   Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA   Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA   Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA   Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA   Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA   Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice chromosome
RT   10.";
RL   Science 300:1566-1569(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=27354554; DOI=10.1105/tpc.16.00265;
RA   Peng M., Gao Y., Chen W., Wang W., Shen S., Shi J., Wang C., Zhang Y.,
RA   Zou L., Wang S., Wan J., Liu X., Gong L., Luo J.;
RT   "Evolutionarily distinct BAHD N-acyltransferases are responsible for
RT   natural variation of aromatic amine conjugates in rice.";
RL   Plant Cell 28:1533-1550(2016).
CC   -!- FUNCTION: Hydroxycinnamoyl transferase that catalyzes the transfer of
CC       an acyl from p-coumaryol-CoA to tryptamine, to produce coumaroyl
CC       tryptamine. Serotonin and tyramine serve as acyl acceptors in vitro.
CC       Can use caffeoyl-CoA, and to a lesser extent feruloyl-CoA, as acyl
CC       donors. {ECO:0000269|PubMed:27354554}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=113.1 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:27354554};
CC         KM=706.3 uM for caffeoyl-CoA {ECO:0000269|PubMed:27354554};
CC         KM=1837 uM for feruloyl-CoA {ECO:0000269|PubMed:27354554};
CC         KM=200.9 uM for tryptamine {ECO:0000269|PubMed:27354554};
CC         KM=130.7 uM for serotonin {ECO:0000269|PubMed:27354554};
CC         KM=199.3 uM for tyramine {ECO:0000269|PubMed:27354554};
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAF26399.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAT10622.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC114474; AAM74310.1; -; Genomic_DNA.
DR   EMBL; DP000086; AAP53439.1; -; Genomic_DNA.
DR   EMBL; AP008216; BAF26399.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP014966; BAT10622.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_015612968.1; XM_015757482.1.
DR   AlphaFoldDB; Q8LMI4; -.
DR   SMR; Q8LMI4; -.
DR   STRING; 4530.OS10T0380100-01; -.
DR   PRIDE; Q8LMI4; -.
DR   GeneID; 4348504; -.
DR   KEGG; osa:4348504; -.
DR   eggNOG; ENOG502QVP8; Eukaryota.
DR   InParanoid; Q8LMI4; -.
DR   OrthoDB; 1130893at2759; -.
DR   SABIO-RK; Q8LMI4; -.
DR   Proteomes; UP000000763; Chromosome 10.
DR   Proteomes; UP000059680; Chromosome 10.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR   GO; GO:0050734; F:hydroxycinnamoyltransferase 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..434
FT                   /note="Tryptamine hydroxycinnamoyltransferase 2"
FT                   /id="PRO_0000437767"
FT   ACT_SITE        154
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT   ACT_SITE        380
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
SQ   SEQUENCE   434 AA;  47107 MW;  3F4C404A35F34F3C CRC64;
     MAVAVEITRS EVLRPSETLA AGGGGKRSQL TVFDRAAMDW YIPAVFAWDG AAAPSNDEVK
     GGLAAVLARY PHLAGRFDVD ERGRRCFNLN NAGVRVLEAT VAADLADALA HDVAAHVNEL
     YPKADMENAD EPVFQVQLTR YACGGLVIGT ACNHQVSDGQ SMSFFYVAWA AAVRSAGATL
     PTPFVDRAAI AVPRGPPAPA FDHRNIEFKG EHSWTHSYGS LPLERIRNLA VHFPDEFVAG
     LKSHVGARCS TFQCLLAHAW KKITAARDLS PEEYTQVRVA VNCRGRASPA VPMDYFGNMV
     LWAFPRMRVR DLLSSSYAAV VGVIRNAVAR VDEQYIQSFV DFGEVAAGDE LTPTAAPPGT
     VFCPDLEVDS WLGFRFHDLD FGRGPPCAFL PPDVPVEGLL IFVPSCAAKG GVEMFMALDD
     VHVEAFRQIC YSMD