SHT_ARATH
ID SHT_ARATH Reviewed; 451 AA.
AC O64470;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Spermidine hydroxycinnamoyl transferase {ECO:0000303|PubMed:19077165};
DE Short=AtSHT {ECO:0000303|PubMed:33519864};
DE EC=2.3.1.- {ECO:0000269|PubMed:19077165};
DE AltName: Full=BAHD-like hydroxycinnamoyl transferase {ECO:0000303|PubMed:19077165};
GN Name=SHT {ECO:0000303|PubMed:19077165};
GN OrderedLocusNames=At2g19070 {ECO:0000312|EMBL:AEC06845.1};
GN ORFNames=T20K24.8 {ECO:0000312|EMBL:AAD12025.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
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]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19077165; DOI=10.1111/j.1365-313x.2008.03773.x;
RA Grienenberger E., Besseau S., Geoffroy P., Debayle D., Heintz D.,
RA Lapierre C., Pollet B., Heitz T., Legrand M.;
RT "A BAHD acyltransferase is expressed in the tapetum of Arabidopsis anthers
RT and is involved in the synthesis of hydroxycinnamoyl spermidines.";
RL Plant J. 58:246-259(2009).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19762055; DOI=10.1016/j.phytochem.2009.08.010;
RA Fellenberg C., Boettcher C., Vogt T.;
RT "Phenylpropanoid polyamine conjugate biosynthesis in Arabidopsis thaliana
RT flower buds.";
RL Phytochemistry 70:1392-1400(2009).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20827470; DOI=10.1007/s00216-010-4129-2;
RA Handrick V., Vogt T., Frolov A.;
RT "Profiling of hydroxycinnamic acid amides in Arabidopsis thaliana pollen by
RT tandem mass spectrometry.";
RL Anal. Bioanal. Chem. 398:2789-2801(2010).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=21849515; DOI=10.1104/pp.111.179523;
RA Dobritsa A.A., Geanconteri A., Shrestha J., Carlson A., Kooyers N.,
RA Coerper D., Urbanczyk-Wochniak E., Bench B.J., Sumner L.W., Swanson R.,
RA Preuss D.;
RT "A large-scale genetic screen in Arabidopsis to identify genes involved in
RT pollen exine production.";
RL Plant Physiol. 157:947-970(2011).
RN [8]
RP FUNCTION.
RX PubMed=22912643; DOI=10.3389/fpls.2012.00180;
RA Fellenberg C., Ziegler J., Handrick V., Vogt T.;
RT "Polyamine homeostasis in wild type and phenolamide deficient Arabidopsis
RT thaliana stamens.";
RL Front. Plant Sci. 3:180-180(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SPERMIDINE AND
RP COENZYME A, AND FUNCTION.
RX PubMed=33519864; DOI=10.3389/fpls.2020.610118;
RA Wang C., Li J., Ma M., Lin Z., Hu W., Lin W., Zhang P.;
RT "Structural and biochemical insights into two BAHD acyltransferases (AtSHT
RT and AtSDT) involved in phenolamide biosynthesis.";
RL Front. Plant Sci. 11:610118-610118(2020).
CC -!- FUNCTION: Hydroxycinnamoyl transferase involved in the conjugation of
CC feruloyl CoA to spermidine (PubMed:19077165, PubMed:19762055,
CC PubMed:33519864). Catalyzes the three conjugating steps required for
CC the biosynthesis of N(1),N(4),N(8)-triferuloyl-spermidine
CC (PubMed:19077165, PubMed:33519864). Spermidine is the only acceptor
CC substrate while feruloyl CoA > caffeoyl CoA > coumaroyl CoA > cinnamoyl
CC CoA >> sinapoyl CoA are efficient acyl donors. No activity with
CC hydroxyferuloyl CoA (PubMed:19077165). Required for the biosynthesis of
CC these conjugated spermidine derivatives, specifically in anther tapetum
CC (PubMed:22912643). {ECO:0000269|PubMed:19077165,
CC ECO:0000269|PubMed:19762055, ECO:0000269|PubMed:22912643,
CC ECO:0000269|PubMed:33519864}.
CC -!- TISSUE SPECIFICITY: Expressed in flower buds and inflorescences.
CC Restricted to anther tapetum. {ECO:0000269|PubMed:19077165,
CC ECO:0000269|PubMed:19762055}.
CC -!- DEVELOPMENTAL STAGE: Expressed during bud growth and diappears when the
CC flower opens. {ECO:0000269|PubMed:19077165}.
CC -!- INDUCTION: Not induced by pathogens or by wounding.
CC {ECO:0000269|PubMed:19077165}.
CC -!- DISRUPTION PHENOTYPE: Glossy and sticky pollen, but very little changes
CC in the exine patterns. Drastic reduction in flower buds of the content
CC in N1,N4,N8-tri-(hydroxyferuloyl)-spermidine and N1,N4-
CC di(hydroxyferuloyl)-N8-sinapoyl-spermidine.
CC {ECO:0000269|PubMed:19077165, ECO:0000269|PubMed:19762055,
CC ECO:0000269|PubMed:20827470, ECO:0000269|PubMed:21849515}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AC002392; AAD12025.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06845.1; -; Genomic_DNA.
DR EMBL; BT002975; AAO22784.1; -; mRNA.
DR EMBL; BT004456; AAO42450.1; -; mRNA.
DR PIR; T00527; T00527.
DR RefSeq; NP_179497.1; NM_127464.2.
DR PDB; 6LPV; X-ray; 2.30 A; A=1-451.
DR PDBsum; 6LPV; -.
DR AlphaFoldDB; O64470; -.
DR SMR; O64470; -.
DR STRING; 3702.AT2G19070.1; -.
DR PaxDb; O64470; -.
DR PRIDE; O64470; -.
DR ProteomicsDB; 232587; -.
DR DNASU; 816424; -.
DR EnsemblPlants; AT2G19070.1; AT2G19070.1; AT2G19070.
DR GeneID; 816424; -.
DR Gramene; AT2G19070.1; AT2G19070.1; AT2G19070.
DR KEGG; ath:AT2G19070; -.
DR Araport; AT2G19070; -.
DR TAIR; locus:2059109; AT2G19070.
DR eggNOG; ENOG502QSYG; Eukaryota.
DR HOGENOM; CLU_014546_2_0_1; -.
DR InParanoid; O64470; -.
DR OMA; KILWAGE; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; O64470; -.
DR BioCyc; ARA:AT2G19070-MON; -.
DR BioCyc; MetaCyc:AT2G19070-MON; -.
DR PRO; PR:O64470; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64470; baseline and differential.
DR Genevisible; O64470; AT.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IBA:GO_Central.
DR GO; GO:0016410; F:N-acyltransferase activity; IDA:TAIR.
DR GO; GO:0080074; F:spermidine:caffeoyl CoA N-acyltransferase activity; IDA:TAIR.
DR GO; GO:0080073; F:spermidine:coumaroyl CoA N-acyltransferase activity; IDA:TAIR.
DR GO; GO:0080075; F:spermidine:feruloyl CoA N-acyltransferase activity; IDA:TAIR.
DR GO; GO:0080072; F:spermidine:sinapoyl CoA N-acyltransferase activity; IDA:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
DR GO; GO:0010584; P:pollen exine formation; IMP:TAIR.
DR GO; GO:0080088; P:spermidine hydroxycinnamate conjugate biosynthetic process; IDA:TAIR.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..451
FT /note="Spermidine hydroxycinnamoyl transferase"
FT /id="PRO_0000419520"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT ACT_SITE 397
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT BINDING 33
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPV"
FT BINDING 155
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPV"
FT BINDING 160
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPV"
FT BINDING 262..263
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPV"
FT BINDING 294
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPV"
FT BINDING 298
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPV"
FT BINDING 314
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPV"
FT BINDING 387
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPV"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 54..68
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:6LPV"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:6LPV"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 160..174
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 187..190
FT /evidence="ECO:0007829|PDB:6LPV"
FT TURN 191..193
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 230..237
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 239..251
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 263..279
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:6LPV"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 312..320
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 321..326
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 345..357
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:6LPV"
FT STRAND 429..436
FT /evidence="ECO:0007829|PDB:6LPV"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:6LPV"
SQ SEQUENCE 451 AA; 50435 MW; B13B2CBF4D4B4482 CRC64;
MAPITFRKSY TIVPAEPTWS GRFPLAEWDQ VGTITHIPTL YFYDKPSESF QGNVVEILKT
SLSRVLVHFY PMAGRLRWLP RGRFELNCNA EGVEFIEAES EGKLSDFKDF SPTPEFENLM
PQVNYKNPIE TIPLFLAQVT KFKCGGISLS VNVSHAIVDG QSALHLISEW GRLARGEPLE
TVPFLDRKIL WAGEPLPPFV SPPKFDHKEF DQPPFLIGET DNVEERKKKT IVVMLPLSTS
QLQKLRSKAN GSKHSDPAKG FTRYETVTGH VWRCACKARG HSPEQPTALG ICIDTRSRME
PPLPRGYFGN ATLDVVAAST SGELISNELG FAASLISKAI KNVTNEYVMI GIEYLKNQKD
LKKFQDLHAL GSTEGPFYGN PNLGVVSWLT LPMYGLDFGW GKEFYTGPGT HDFDGDSLIL
PDQNEDGSVI LATCLQVAHM EAFKKHFYED I
