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AT4_ORYSJ
ID   AT4_ORYSJ               Reviewed;         439 AA.
AC   Q5JNT2;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Acyl transferase 4 {ECO:0000305};
DE            Short=OsAT4 {ECO:0000303|PubMed:23391577};
DE            EC=2.3.1.- {ECO:0000305};
DE   AltName: Full=p-coumaroyl-CoA monolignol transferase {ECO:0000305};
DE            Short=OsPMT {ECO:0000303|PubMed:22267741};
GN   Name=AT4 {ECO:0000303|PubMed:23391577};
GN   Synonyms=PMT {ECO:0000303|PubMed:22267741};
GN   OrderedLocusNames=Os01g0291500 {ECO:0000312|EMBL:BAS71658.1},
GN   LOC_Os01g18744 {ECO:0000305};
GN   ORFNames=OsJ_01392 {ECO:0000312|EMBL:EAZ11526.1},
GN   P0706B05.17 {ECO:0000312|EMBL:BAD86875.1};
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=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
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   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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=22267741; DOI=10.1074/jbc.m111.284497;
RA   Withers S., Lu F., Kim H., Zhu Y., Ralph J., Wilkerson C.G.;
RT   "Identification of grass-specific enzyme that acylates monolignols with p-
RT   coumarate.";
RL   J. Biol. Chem. 287:8347-8355(2012).
RN   [8]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=23391577; DOI=10.1104/pp.112.208694;
RA   Bartley L.E., Peck M.L., Kim S.R., Ebert B., Manisseri C., Chiniquy D.M.,
RA   Sykes R., Gao L., Rautengarten C., Vega-Sanchez M.E., Benke P.I.,
RA   Canlas P.E., Cao P., Brewer S., Lin F., Smith W.L., Zhang X.,
RA   Keasling J.D., Jentoff R.E., Foster S.B., Zhou J., Ziebell A., An G.,
RA   Scheller H.V., Ronald P.C.;
RT   "Overexpression of a BAHD acyltransferase, OsAt10, alters rice cell wall
RT   hydroxycinnamic acid content and saccharification.";
RL   Plant Physiol. 161:1615-1633(2013).
CC   -!- FUNCTION: Grass-specific monolignol p-coumaroyl transferase involved in
CC       the biosynthesis of acylated monolignols or monolignol conjugates that
CC       serve as monomer precursors of lignin. Can synthesize sinapyl p-
CC       coumarate, p-coumaryl p-coumarate, sinapyl caffeate and p-coumaryl
CC       caffeate in vitro. {ECO:0000269|PubMed:22267741}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=35 uM for sinapyl alcohol {ECO:0000269|PubMed:22267741};
CC         KM=105 uM for p-coumaroyl-CoA {ECO:0000269|PubMed:22267741};
CC         KM=141 uM for p-coumaryl alcohol {ECO:0000269|PubMed:22267741};
CC         Vmax=10.8 nmol/sec/mg enzyme toward sinapyl alcohol
CC         {ECO:0000269|PubMed:22267741};
CC         Vmax=12.5 nmol/sec/mg enzyme toward p-coumaroyl-CoA
CC         {ECO:0000269|PubMed:22267741};
CC         Vmax=54.2 nmol/sec/mg enzyme toward p-coumaryl alcohol
CC         {ECO:0000269|PubMed:22267741};
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; AP002482; BAD86875.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF04705.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS71658.1; -; Genomic_DNA.
DR   EMBL; CM000138; EAZ11526.1; -; Genomic_DNA.
DR   EMBL; AK060689; BAG87540.1; -; mRNA.
DR   EMBL; AK070443; BAG91955.1; -; mRNA.
DR   RefSeq; XP_015621300.1; XM_015765814.1.
DR   AlphaFoldDB; Q5JNT2; -.
DR   SMR; Q5JNT2; -.
DR   STRING; 4530.OS01T0291500-01; -.
DR   PaxDb; Q5JNT2; -.
DR   PRIDE; Q5JNT2; -.
DR   EnsemblPlants; Os01t0291500-01; Os01t0291500-01; Os01g0291500.
DR   EnsemblPlants; Os01t0291500-02; Os01t0291500-02; Os01g0291500.
DR   GeneID; 4325160; -.
DR   Gramene; Os01t0291500-01; Os01t0291500-01; Os01g0291500.
DR   Gramene; Os01t0291500-02; Os01t0291500-02; Os01g0291500.
DR   KEGG; osa:4325160; -.
DR   eggNOG; ENOG502QQHA; Eukaryota.
DR   HOGENOM; CLU_014546_2_0_1; -.
DR   InParanoid; Q5JNT2; -.
DR   OMA; VHVVPIQ; -.
DR   OrthoDB; 1130893at2759; -.
DR   SABIO-RK; Q5JNT2; -.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   GO; GO:0050734; F:hydroxycinnamoyltransferase activity; IEA:UniProt.
DR   GO; GO:0016410; F:N-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0009809; P:lignin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Lignin biosynthesis; Reference proteome; Transferase.
FT   CHAIN           1..439
FT                   /note="Acyl transferase 4"
FT                   /id="PRO_0000437775"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
FT   ACT_SITE        382
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q8W1W9"
SQ   SEQUENCE   439 AA;  46885 MW;  EA2DD1CEF770D145 CRC64;
     MGFAVVRTNR EFVRPSAATP PSSGELLELS IIDRVVGLRH LVRSLHIFSA AAPSGGDAKP
     SPARVIKEAL GKALVDYYPF AGRFVDGGGG PGSARVECTG EGAWFVEAAA GCSLDDVNGL
     DHPLMIPEDD LLPDAAPGVH PLDLPLMMQV TEFSCGGFVV GLISVHTMAD GLGAGQFINA
     VGDYARGLDR PRVSPVWARE AIPSPPKLPP GPPPELKMFQ LRHVTADLSL DSINKAKSAY
     FAATGHRCST FDVAIAKTWQ ARTRALRLPE PTSRVNLCFF ANTRHLMAGA AAWPAPAAGG
     NGGNGFYGNC FYPVSVVAES GAVEAADVAG VVGMIREAKA RLPADFARWA VADFREDPYE
     LSFTYDSLFV SDWTRLGFLE ADYGWGPPSH VIPFAYYPFM AVAIIGAPPV PKTGARIMTQ
     CVEDDHLPAF KEEIKAFDK
 
 
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