PUHT_ORYSJ
ID PUHT_ORYSJ Reviewed; 452 AA.
AC Q7XXN4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putrescine hydroxycinnamoyltransferase {ECO:0000305|PubMed:24908251};
DE EC=2.3.1.- {ECO:0000305};
GN OrderedLocusNames=Os09g0544000 {ECO:0000312|EMBL:BAT09226.1},
GN LOC_Os09g37200 {ECO:0000305};
GN ORFNames=OsJ_30201 {ECO:0000312|EMBL:EAZ45541.1},
GN P0705E11.4 {ECO:0000312|EMBL:BAC79155.1};
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=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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP FUNCTION.
RX PubMed=24908251; DOI=10.1038/ng.3007;
RA Chen W., Gao Y., Xie W., Gong L., Lu K., Wang W., Li Y., Liu X., Zhang H.,
RA Dong H., Zhang W., Zhang L., Yu S., Wang G., Lian X., Luo J.;
RT "Genome-wide association analyses provide genetic and biochemical insights
RT into natural variation in rice metabolism.";
RL Nat. Genet. 46:714-721(2014).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION
RP BY WOUNDING.
RX PubMed=27015846; DOI=10.1111/jipb.12480;
RA Tanabe K., Hojo Y., Shinya T., Galis I.;
RT "Molecular evidence for biochemical diversification of phenolamide
RT biosynthesis in rice plants.";
RL J. Integr. Plant Biol. 58:903-913(2016).
CC -!- FUNCTION: Hydroxycinnamoyl transferase that catalyzes the transfer of
CC an acyl from p-coumaryol-CoA to putrescine, to produce coumaroyl
CC putrescine. Can use feruloyl-CoA, caffeoyl-CoA and sinapoyl-CoA as acyl
CC donors. Seems to be able to transfer the acyl group from feruloyl-CoA
CC to the acyl acceptors agmatine and spermidine.
CC {ECO:0000269|PubMed:24908251, ECO:0000269|PubMed:27015846}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37.3 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:27015846};
CC KM=35.6 uM for feruloyl-CoA {ECO:0000269|PubMed:27015846};
CC KM=66.1 uM for putrescine {ECO:0000269|PubMed:27015846};
CC KM=322 uM for agmatine {ECO:0000269|PubMed:27015846};
CC -!- TISSUE SPECIFICITY: Highly expressed in roots. Expressed at low levels
CC in flowers. {ECO:0000269|PubMed:27015846}.
CC -!- INDUCTION: By wounding. {ECO:0000269|PubMed:27015846}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AP006548; BAC79155.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF25743.1; -; Genomic_DNA.
DR EMBL; AP014965; BAT09226.1; -; Genomic_DNA.
DR EMBL; CM000146; EAZ45541.1; -; Genomic_DNA.
DR RefSeq; XP_015651357.1; XM_015795871.1.
DR AlphaFoldDB; Q7XXN4; -.
DR SMR; Q7XXN4; -.
DR STRING; 39947.Q7XXN4; -.
DR PaxDb; Q7XXN4; -.
DR PRIDE; Q7XXN4; -.
DR EnsemblPlants; Os09t0544000-01; Os09t0544000-01; Os09g0544000.
DR GeneID; 4347748; -.
DR Gramene; Os09t0544000-01; Os09t0544000-01; Os09g0544000.
DR KEGG; osa:4347748; -.
DR eggNOG; ENOG502QTU2; Eukaryota.
DR HOGENOM; CLU_014546_6_2_1; -.
DR InParanoid; Q7XXN4; -.
DR OMA; WGKACRG; -.
DR OrthoDB; 1130893at2759; -.
DR BRENDA; 2.3.1.138; 8948.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
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..452
FT /note="Putrescine hydroxycinnamoyltransferase"
FT /id="PRO_0000437770"
FT REGION 213..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT ACT_SITE 398
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8W1W9"
SQ SEQUENCE 452 AA; 48612 MW; EAA6B8B77C118B50 CRC64;
MEVKVLSSRL VRPSYPASAA APEEEFVPSS MFDKVTYDMQ MAIIYAFRPP GPSVADIEKG
LAAVLGVYRL FAGQVVRGGG GELRGVVLND HGARLVEACV DGSLADIAPA KPSPVVLRLH
PSLEGEIEEV VQVQLTRFAC GSLAVGFTAN HAVADGHATS DFLVAWGRAA RGLAVAATAA
APPHHHPGMF RPRDPPLVEF EHRGVEYYRP PPPAAGVDGD VGGDHKQQHG HGGEEASHGI
VIHKAHFTKD FIARLRAAAS EGRGRPFSRF ETILAHVWRT MTRARGLGNP LQSSTIRISV
DGRQRLSAPA GYFGNLVLWA FPRATVGDLL GRPLKHAAQV IHDAVARADA AYFRSFVDFA
SSGAVEGEGL APTAVLKDVL CPDLEVDSWL TFPFYELDFG GGCPTYFMPS YFPTEGMLFL
VPSYLGDGSV DAFVPVFDHN LEAFKQSCYS IE
