3AT1_ARATH
ID 3AT1_ARATH Reviewed; 469 AA.
AC Q9ZWB4;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Coumaroyl-CoA:anthocyanidin 3-O-glucoside-6''-O-coumaroyltransferase 1;
DE EC=2.3.1.-;
GN Name=3AT1; OrderedLocusNames=At1g03940; ORFNames=F21M11.13;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=17425720; DOI=10.1111/j.1365-313x.2007.03079.x;
RA Luo J., Nishiyama Y., Fuell C., Taguchi G., Elliott K., Hill L., Tanaka Y.,
RA Kitayama M., Yamazaki M., Bailey P., Parr A., Michael A.J., Saito K.,
RA Martin C.;
RT "Convergent evolution in the BAHD family of acyl transferases:
RT identification and characterization of anthocyanin acyl transferases from
RT Arabidopsis thaliana.";
RL Plant J. 50:678-695(2007).
RN [4]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=23473981; DOI=10.1016/j.plaphy.2013.02.001;
RA Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M.,
RA Tohge T., Fernie A.R.;
RT "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic
RT diversity.";
RL Plant Physiol. Biochem. 72:21-34(2013).
CC -!- FUNCTION: Involved in the acylation of the 6'' position of the 3-O-
CC glucose residue of anthocyanin. Also able to use flavonol 3-glucosides
CC as the acyl acceptor. {ECO:0000269|PubMed:17425720}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.9 uM for p-coumaroyl-CoA (with cyanidin 3,5-diglucoside as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC KM=4.2 uM for feruloyl-CoA (with cyanidin 3,5-diglucoside as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC KM=2.2 uM for caffeoyl-CoA (with cyanidin 3,5-diglucoside as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC KM=7.0 uM for cyanidin 3-glucoside (with malonyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:17425720};
CC KM=7.3 uM for pelargonidin 3-glucoside (with malonyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC KM=6.9 uM for malvidin 3-glucoside (with malonyl-CoA as cosubstrate)
CC {ECO:0000269|PubMed:17425720};
CC KM=45.7 uM for quercetin 3-glucoside (with malonyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC KM=64.8 uM for kaempferol 3-glucoside (with malonyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC KM=9.4 uM for kaempferol 7-glucoside (with malonyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC KM=141 uM for cyanidin 3,5-diglucoside (with malonyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC KM=116 uM for pelargonidin 3,5-diglucoside (with malonyl-CoA as
CC cosubstrate) {ECO:0000269|PubMed:17425720};
CC Note=kcat is 7.6 sec(-1) for p-coumaroyl-CoA. kcat is 8.5 sec(-1) for
CC feruloyl-CoA. kcat is 9.3 sec(-1) for caffeoyl-CoA. kcat is 7.6 sec(-
CC 1) for cyanidin 3-glucoside. kcat is 8.0 sec(-1) for pelargonidin 3-
CC glucoside. kcat is 7.8 sec(-1) for malvidin 3-glucoside. kcat is 1.2
CC sec(-1) for quercetin 3-glucoside. kcat is 1.1 sec(-1) for kaempferol
CC 3-glucoside. kcat is 2.6 sec(-1) for kaempferol 7-glucoside. kcat is
CC <0.001 sec(-1) for cyanidin 3,5-diglucoside. kcat is <0.001 sec(-1)
CC for pelargonidin 3,5-diglucoside.;
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers, leaves and roots.
CC Lower levels of expression in stems and siliques.
CC {ECO:0000269|PubMed:17425720}.
CC -!- INDUCTION: Up-regulated by high sucrose and by low phosphate stresses.
CC {ECO:0000269|PubMed:17425720}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, probably due to the
CC redundancy with 3AT2. {ECO:0000269|PubMed:17425720}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AC003027; AAD10676.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27636.1; -; Genomic_DNA.
DR PIR; C86170; C86170.
DR RefSeq; NP_171890.1; NM_100275.3.
DR AlphaFoldDB; Q9ZWB4; -.
DR SMR; Q9ZWB4; -.
DR STRING; 3702.AT1G03940.1; -.
DR PaxDb; Q9ZWB4; -.
DR PRIDE; Q9ZWB4; -.
DR ProteomicsDB; 245166; -.
DR EnsemblPlants; AT1G03940.1; AT1G03940.1; AT1G03940.
DR GeneID; 839366; -.
DR Gramene; AT1G03940.1; AT1G03940.1; AT1G03940.
DR KEGG; ath:AT1G03940; -.
DR Araport; AT1G03940; -.
DR TAIR; locus:2024127; AT1G03940.
DR eggNOG; ENOG502QPXT; Eukaryota.
DR HOGENOM; CLU_014546_7_2_1; -.
DR OMA; HERDKVK; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; Q9ZWB4; -.
DR BioCyc; ARA:AT1G03940-MON; -.
DR BioCyc; MetaCyc:MON-18503; -.
DR PRO; PR:Q9ZWB4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZWB4; baseline and differential.
DR Genevisible; Q9ZWB4; AT.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..469
FT /note="Coumaroyl-CoA:anthocyanidin 3-O-glucoside-6''-O-
FT coumaroyltransferase 1"
FT /id="PRO_0000419540"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 410
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q940Z5"
SQ SEQUENCE 469 AA; 51926 MW; FE5CC01DBB80CC21 CRC64;
MVAHLQPPKI IETCHISPPK GTVPSTTLPL TFFDAPWLSL PLADSLFFFS YQNSTESFLQ
DFVPNLKHSL SITLQHFFPY AGKLIIPPRP DPPYLHYNDG QDSLVFTVAE STETDFDQLK
SDSPKDISVL HGVLPKLPPP HVSPEGIQMR PIMAMQVTIF PGAGICIGNS ATHVVADGVT
FSHFMKYWMS LTKSSGKDPA TVLLPSLPIH SCRNMIKDPG EVGAGHLERF WSQNSAKHSS
HVTPENMVRA TFTLSRKQID NLKSWVTEQS ENQSPVSTFV VTLAFIWVSL IKTLVQDSET
KANEEDKDEV FHLMINVDCR NRLKYTQPIP QTYFGNCMAP GIVSVKKHDL LGEKCVLAAS
DAITARIKDM LSSDLLKTAP RWGQGVRKWV MSHYPTSIAG APKLGLYDMD FGLGKPCKME
IVHIETGGSI AFSESRDGSN GVEIGIALEK KKMDVFDSIL QQGIKKFAT
