SCT_ARATH
ID SCT_ARATH Reviewed; 461 AA.
AC Q8GYW8;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Spermidine coumaroyl-CoA acyltransferase {ECO:0000303|PubMed:19168716};
DE Short=SCT {ECO:0000303|PubMed:19168716};
DE Short=Spermidine dicoumaroyl transferase {ECO:0000303|PubMed:19168716};
DE EC=2.3.1.249 {ECO:0000269|PubMed:19168716};
GN Name=SCT {ECO:0000303|PubMed:19168716};
GN OrderedLocusNames=At2g25150 {ECO:0000312|Araport:AT2G25150};
GN ORFNames=F13D4.110;
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|EMBL:BAC42015.1};
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CATALYTIC ACTIVITY.
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).
CC -!- FUNCTION: Spermidine coumaroyl-CoA acyltransferase that mediates the
CC conversion of spermidine into dicoumaroyl-spermidine.
CC {ECO:0000269|PubMed:19168716}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (E)-4-coumaroyl-CoA + spermidine = 2 CoA + 2 H(+) +
CC N(1),N(8)-bis(coumaroyl)-spermidine; Xref=Rhea:RHEA:45180,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57834,
CC ChEBI:CHEBI:85007, ChEBI:CHEBI:85008; EC=2.3.1.249;
CC Evidence={ECO:0000269|PubMed:19168716};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.6 uM for coumaroyl-CoA (with spermidine as the acyl acceptor,
CC at 30 degrees Celsius) {ECO:0000269|PubMed:19168716};
CC KM=52.7 uM for spermidine (with sinapoyl-CoA as the acyl donor, at 30
CC degrees Celsius) {ECO:0000269|PubMed:19168716};
CC Note=kcat is 3.4 sec(-1) with coumaroyl-CoA as substrate (in the
CC presence of spermidine as the acyl acceptor). kcat is 3.1 sec(-1)
CC with spermidin as substrate (in the presence of coumaroyl-CoA as the
CC acyl donor). All analyses are done at 30 degrees Celsius.
CC {ECO:0000269|PubMed:19168716};
CC pH dependence:
CC Optimum pH is 9 using spermidine and coumaroyl-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: Mainly expressed in roots at low levels,
CC specifically, in the root tip. {ECO:0000269|PubMed:19168716}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; CP002685; AEC07663.1; -; Genomic_DNA.
DR EMBL; AK117345; BAC42015.1; -; mRNA.
DR EMBL; BT009686; AAP81804.1; -; mRNA.
DR PIR; H84644; H84644.
DR RefSeq; NP_180087.1; NM_128072.3.
DR AlphaFoldDB; Q8GYW8; -.
DR SMR; Q8GYW8; -.
DR STRING; 3702.AT2G25150.1; -.
DR iPTMnet; Q8GYW8; -.
DR PaxDb; Q8GYW8; -.
DR PRIDE; Q8GYW8; -.
DR EnsemblPlants; AT2G25150.1; AT2G25150.1; AT2G25150.
DR GeneID; 817053; -.
DR Gramene; AT2G25150.1; AT2G25150.1; AT2G25150.
DR KEGG; ath:AT2G25150; -.
DR Araport; AT2G25150; -.
DR TAIR; locus:2040169; AT2G25150.
DR eggNOG; ENOG502QV0F; Eukaryota.
DR HOGENOM; CLU_014546_2_0_1; -.
DR InParanoid; Q8GYW8; -.
DR OMA; MTWNHVV; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q8GYW8; -.
DR BioCyc; ARA:AT2G25150-MON; -.
DR BRENDA; 2.3.1.249; 399.
DR UniPathway; UPA00819; -.
DR PRO; PR:Q8GYW8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8GYW8; baseline and differential.
DR Genevisible; Q8GYW8; AT.
DR GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0080073; F:spermidine:coumaroyl CoA N-acyltransferase activity; IDA:UniProtKB.
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 Acyltransferase; Polyamine biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..461
FT /note="Spermidine coumaroyl-CoA acyltransferase"
FT /id="PRO_0000432772"
FT ACT_SITE 168
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
FT ACT_SITE 393
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q70PR7"
SQ SEQUENCE 461 AA; 51751 MW; 435F70EB768595BD CRC64;
MANQRKPILP LLLEKKPVEL VKPSKHTHCE TLSLSTLDND PFNEVMYATI YVFKANGKNL
DDPVSLLRKA LSELLVHYYP LSGKLMRSES NGKLQLVYLG EGVPFEVATS TLDLSSLNYI
ENLDDQVALR LVPEIEIDYE SNVCYHPLAL QVTKFACGGF TIGTALTHAV CDGYGVAQII
HALTELAAGK TEPSVKSVWQ RERLVGKIDN KPGKVPGSHI DGFLATSAYL PTTDVVTETI
NIRAGDIKRL KDSMMKECEY LKESFTTYEV LSSYIWKLRS RALKLNPDGI TVLGVAVGIR
HVLDPPLPKG YYGNAYIDVY VELTVRELEE SSISNIANRV KKAKKTAYEK GYIEEELKNT
ERLMRDDSMF EGVSDGLFFL TDWRNIGWFG SMDFGWNEPV NLRPLTQRES TVHVGMILKP
SKSDPSMEGG VKVIMKLPRD AMVEFKREMA TMKKLYFGDT N
