SDT_ARATH
ID SDT_ARATH Reviewed; 451 AA.
AC O80467;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Spermidine sinapoyl-CoA acyltransferase {ECO:0000303|PubMed:19168716};
DE Short=AtSDT {ECO:0000303|PubMed:33519864};
DE Short=Spermidine disinapoyl transferase {ECO:0000303|PubMed:19168716};
DE EC=2.3.1.248 {ECO:0000269|PubMed:19168716};
GN Name=SDT {ECO:0000303|PubMed:19168716};
GN OrderedLocusNames=At2g23510 {ECO:0000312|Araport:AT2G23510};
GN ORFNames=F26B6.16 {ECO:0000312|EMBL:AAC23766.1};
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 {ECO:0000312|Proteomes:UP000006548};
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 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia;
RX PubMed=19168716; DOI=10.1105/tpc.108.063511;
RA Luo J., Fuell C., Parr A., Hill L., Bailey P., Elliott K., Fairhurst S.A.,
RA Martin C., Michael A.J.;
RT "A novel polyamine acyltransferase responsible for the accumulation of
RT spermidine conjugates in Arabidopsis seed.";
RL Plant Cell 21:318-333(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS)IN COMPLEX WITH SPERMIDINE, AND
RP 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: Spermidine sinapoyl-CoA acyltransferase that mediates the
CC accumulation of disinapoyl spermidine conjugates in seeds
CC (PubMed:19168716). Catalyzes the two conjugating steps required for the
CC biosynthesis of N1,N8-disipanoyl-spermidine (PubMed:19168716,
CC PubMed:33519864). Can also use putrescine as an acyl acceptor to
CC convert it into monosinapoyl-putrescine (PubMed:19168716).
CC {ECO:0000269|PubMed:19168716, ECO:0000269|PubMed:33519864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (E)-sinapoyl-CoA + spermidine = 2 CoA + 2 H(+) + N(1),N(8)-
CC bis[(E)-sinapoyl]-spermidine; Xref=Rhea:RHEA:45168,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57393,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:85006; EC=2.3.1.248;
CC Evidence={ECO:0000269|PubMed:19168716};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.3 uM for sinapoyl-CoA (with spermidine as the acyl acceptor, at
CC 30 degrees Celsius) {ECO:0000269|PubMed:19168716};
CC KM=37.4 uM for spermidine (with sinapoyl-CoA as the acyl donor, at 30
CC degrees Celsius) {ECO:0000269|PubMed:19168716};
CC KM=236.9 uM for putrescine (with sinapoyl-CoA as the acyl donor, at
CC 30 degrees Celsius) {ECO:0000269|PubMed:19168716};
CC KM=34.6 uM for disinapoyl-spermidine (with CoA as cosubstrate, at 30
CC degrees Celsius) {ECO:0000269|PubMed:19168716};
CC KM=83.6 uM for CoA (with disinapoyl-spermidine as cosubstrate, at 30
CC degrees Celsius) {ECO:0000269|PubMed:19168716};
CC Note=kcat is 5.1 sec(-1) with sinapoyl-CoA as substrate (in the
CC presence of spermidine as the acyl acceptor). kcat is 5.6 sec(-1)
CC with spermidine as substrate (in the presence of sinapoyl-CoA as the
CC acyl donor). kcat is 0.3 sec(-1) with putrescine as substrate (in the
CC presence of sinapoyl-CoA as the acyl donor). kcat is 37.8 sec(-1)
CC with disinapoyl-spermidine as substrate (in the presence of CoA as
CC cosubstrate). kcat is 39.6 sec(-1) with CoA as substrate (in the
CC presence of disinapoyl-spermidine as cosubstrate). All analyses are
CC done at 30 degrees Celsius. {ECO:0000269|PubMed:19168716};
CC pH dependence:
CC Optimum pH is 9 using spermidine and sinapoyl-CoA as substrates.
CC {ECO:0000269|PubMed:19168716};
CC -!- PATHWAY: Amine and polyamine metabolism; spermidine metabolism.
CC {ECO:0000269|PubMed:19168716}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9M6E2}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in siliques, especially in
CC seeds around the embryo, and, at low levels, in flowers. Barely
CC detectable in stems, leaves, and roots. {ECO:0000269|PubMed:19168716}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in the cotyledons and emerging
CC radical of the germinating seeds one day after imbibition. Accumulates
CC in the root tip of young seedlings and in the cotyledons and the basal
CC region of the hypocotyl as the seedlings emerges from the seed coat
CC three days after imbibition. Later confined to the basal region of the
CC hypocotyls and to the root tip before progressively disappearing.
CC {ECO:0000269|PubMed:19168716}.
CC -!- DISRUPTION PHENOTYPE: Impaired disinapoyl spermidine conjugates
CC accumulation in seeds. {ECO:0000269|PubMed:19168716}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AC003040; AAC23766.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07460.1; -; Genomic_DNA.
DR PIR; T01140; T01140.
DR RefSeq; NP_179932.1; NM_127915.2.
DR PDB; 6LPW; X-ray; 2.40 A; A/B=1-451.
DR PDBsum; 6LPW; -.
DR AlphaFoldDB; O80467; -.
DR SMR; O80467; -.
DR STRING; 3702.AT2G23510.1; -.
DR PaxDb; O80467; -.
DR PRIDE; O80467; -.
DR ProteomicsDB; 232827; -.
DR EnsemblPlants; AT2G23510.1; AT2G23510.1; AT2G23510.
DR GeneID; 816883; -.
DR Gramene; AT2G23510.1; AT2G23510.1; AT2G23510.
DR KEGG; ath:AT2G23510; -.
DR Araport; AT2G23510; -.
DR TAIR; locus:2046822; AT2G23510.
DR eggNOG; ENOG502RBEP; Eukaryota.
DR HOGENOM; CLU_014546_2_0_1; -.
DR InParanoid; O80467; -.
DR OMA; SKKMPIC; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; O80467; -.
DR BioCyc; ARA:AT2G23510-MON; -.
DR BRENDA; 2.3.1.248; 399.
DR UniPathway; UPA00819; -.
DR PRO; PR:O80467; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80467; baseline and differential.
DR Genevisible; O80467; AT.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0080089; F:sinapoyl spermidine:sinapoyl CoA N-acyltransferase activity; IDA:TAIR.
DR GO; GO:0080072; F:spermidine:sinapoyl CoA N-acyltransferase activity; IDA:TAIR.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008216; P:spermidine metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Polyamine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..451
FT /note="Spermidine sinapoyl-CoA acyltransferase"
FT /id="PRO_0000432771"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT ACT_SITE 391
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT BINDING 47
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPW"
FT BINDING 169
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPW"
FT BINDING 294
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPW"
FT BINDING 316
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPW"
FT BINDING 378
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:33519864,
FT ECO:0007744|PDB:6LPW"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 65..79
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:6LPW"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:6LPW"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:6LPW"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:6LPW"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 314..322
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 331..345
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 348..364
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:6LPW"
FT TURN 406..411
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:6LPW"
FT STRAND 429..436
FT /evidence="ECO:0007829|PDB:6LPW"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:6LPW"
SQ SEQUENCE 451 AA; 50377 MW; AD66D1D7F751DE74 CRC64;
MPIHIGSSIP LMVEKMLTEM VKPSKHIPQQ TLNLSTLDND PYNEVIYKAC YVFKAKNVAD
DDNRPEALLR EALSDLLGYY YPLSGSLKRQ ESDRKLQLSC GGDGGGVPFT VATANVELSS
LKNLENIDSD TALNFLPVLH VDIDGYRPFA LQVTKFECGG FILGMAMSHA MCDGYGEGHI
MCALTDLAGG KKKPMVTPIW ERERLVGKPE DDQPPFVPGD DTAASPYLPT DDWVTEKITI
RADSIRRLKE ATLKEYDFSN ETITTFEVIG AYLWKSRVKA LNLDRDGVTV LGLSVGIRNV
VDPPLPDGYY GNAYIDMYVP LTAREVEEFT ISDIVKLIKE AKRNAHDKDY LQEELANTEK
IIKMNLTIKG KKDGLFCLTD WRNIGIFGSM DFGWDEPVNI VPVVPSETAR TVNMFMRPSR
LESDMVGGVQ IVVTLPRIAM VKFKEEMEAL E
