CFAT_PETHY
ID CFAT_PETHY Reviewed; 454 AA.
AC A1XWY7;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Coniferyl alcohol acyltransferase {ECO:0000303|PubMed:17241449};
DE Short=PhCFAT {ECO:0000303|PubMed:17241449};
DE EC=2.3.1.- {ECO:0000269|PubMed:17241449};
DE AltName: Full=(E)-cinnamyl alcohol acyltransferase {ECO:0000303|PubMed:17241449};
DE EC=2.3.1.224 {ECO:0000269|PubMed:17241449};
DE AltName: Full=(E)-sinapoyl alcohol acyltransferase {ECO:0000303|PubMed:17241449};
DE EC=2.3.1.- {ECO:0000269|PubMed:17241449};
DE AltName: Full=Geraniol acyltransferase {ECO:0000303|PubMed:17241449};
DE EC=2.3.1.- {ECO:0000269|PubMed:17241449};
DE AltName: Full=Octan-1-ol acyltransferase {ECO:0000303|PubMed:17241449};
DE EC=2.3.1.- {ECO:0000269|PubMed:17241449};
GN Name=CFAT {ECO:0000303|PubMed:17241449};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP INDUCTION, PATHWAY, AND DEVELOPMENTAL STAGE.
RX PubMed=17241449; DOI=10.1111/j.1365-313x.2006.02954.x;
RA Dexter R., Qualley A., Kish C.M., Ma C.J., Koeduka T., Nagegowda D.A.,
RA Dudareva N., Pichersky E., Clark D.;
RT "Characterization of a petunia acetyltransferase involved in the
RT biosynthesis of the floral volatile isoeugenol.";
RL Plant J. 49:265-275(2007).
RN [2]
RP INDUCTION BY EOBII, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Violet 26;
RX PubMed=20543029; DOI=10.1105/tpc.109.067280;
RA Spitzer-Rimon B., Marhevka E., Barkai O., Marton I., Edelbaum O., Masci T.,
RA Prathapani N.K., Shklarman E., Ovadis M., Vainstein A.;
RT "EOBII, a gene encoding a flower-specific regulator of phenylpropanoid
RT volatiles' biosynthesis in petunia.";
RL Plant Cell 22:1961-1976(2010).
RN [3]
RP INDUCTION.
RX PubMed=26124104; DOI=10.1073/pnas.1422875112;
RA Fenske M.P., Hewett Hazelton K.D., Hempton A.K., Shim J.S., Yamamoto B.M.,
RA Riffell J.A., Imaizumi T.;
RT "Circadian clock gene LATE ELONGATED HYPOCOTYL directly regulates the
RT timing of floral scent emission in Petunia.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:9775-9780(2015).
CC -!- FUNCTION: Acyltransferase involved in the biosynthesis of the floral
CC volatile isoeugenol, and which promotes the formation of
CC phenylacetaldehyde, phenylethyl alcohol, phenyl-ethyl acetate,
CC phenylethyl benzoate and benzyl acetate (PubMed:17241449). Catalyzes
CC the acetylation of coniferyl alcohol to produce coniferyl acetate
CC (PubMed:17241449). Also active toward 1-octanol, cinnamyl alcohol,
CC geraniol and sinapyl alcohol (PubMed:17241449).
CC {ECO:0000269|PubMed:17241449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-coniferol + acetyl-CoA = (E)-coniferyl acetate + CoA;
CC Xref=Rhea:RHEA:64616, ChEBI:CHEBI:17745, ChEBI:CHEBI:47905,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
CC Evidence={ECO:0000269|PubMed:17241449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64617;
CC Evidence={ECO:0000269|PubMed:17241449};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-cinnamyl alcohol + acetyl-CoA = (E)-cinnamyl acetate +
CC CoA; Xref=Rhea:RHEA:36151, ChEBI:CHEBI:33227, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:156069; EC=2.3.1.224;
CC Evidence={ECO:0000269|PubMed:17241449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36152;
CC Evidence={ECO:0000269|PubMed:17241449};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geraniol + acetyl-CoA = (2E)-geranyl acetate + CoA;
CC Xref=Rhea:RHEA:64624, ChEBI:CHEBI:5331, ChEBI:CHEBI:17447,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
CC Evidence={ECO:0000269|PubMed:17241449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64625;
CC Evidence={ECO:0000269|PubMed:17241449};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + octan-1-ol = CoA + octyl acetate;
CC Xref=Rhea:RHEA:64628, ChEBI:CHEBI:16188, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:87495;
CC Evidence={ECO:0000269|PubMed:17241449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64629;
CC Evidence={ECO:0000269|PubMed:17241449};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-sinapyl alcohol + acetyl-CoA = (E)-sinapoyl actetate +
CC CoA; Xref=Rhea:RHEA:64620, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:64557, ChEBI:CHEBI:156067;
CC Evidence={ECO:0000269|PubMed:17241449};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64621;
CC Evidence={ECO:0000269|PubMed:17241449};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=56.5 uM for coniferyl alcohol (in the presence of acetyl CoA and
CC at pH 6) {ECO:0000269|PubMed:17241449};
CC KM=30.6 uM for acetyl CoA (in the presence of coniferyl alcohol and
CC at pH 6) {ECO:0000269|PubMed:17241449};
CC KM=27.5 uM for coniferyl alcohol (in the presence of acetyl CoA and
CC at pH 7.5) {ECO:0000269|PubMed:17241449};
CC KM=44.1 uM for acetyl CoA (in the presence of coniferyl alcohol and
CC at pH 7.5) {ECO:0000269|PubMed:17241449};
CC KM=4500 uM for benzyl alcohol (in the presence of acetyl CoA and at
CC pH 7.5) {ECO:0000269|PubMed:17241449};
CC KM=22.6 uM for acetyl CoA (in the presence of benzyl alcohol and at
CC pH 7.5) {ECO:0000269|PubMed:17241449};
CC KM=3600 uM for 2-phenyl ethanol (in the presence of acetyl CoA and at
CC pH 7.5) {ECO:0000269|PubMed:17241449};
CC KM=45.1 uM for acetyl CoA (in the presence of 2-phenyl ethanol and at
CC pH 7.5) {ECO:0000269|PubMed:17241449};
CC Vmax=40.1 nmol/sec/mg enzyme with coniferyl alcohol as substrate (in
CC the presence of acetyl CoA and at pH 6)
CC {ECO:0000269|PubMed:17241449};
CC Vmax=45.3 nmol/sec/mg enzyme with acetyl CoA as substrate (in the
CC presence of coniferyl alcohol and at pH 6)
CC {ECO:0000269|PubMed:17241449};
CC Vmax=15.9 nmol/sec/mg enzyme with coniferyl alcohol as substrate (in
CC the presence of acetyl CoA and at pH 7.5)
CC {ECO:0000269|PubMed:17241449};
CC Vmax=29.5 nmol/sec/mg enzyme with acetyl CoA as substrate (in the
CC presence of coniferyl alcohol and at pH 7.5)
CC {ECO:0000269|PubMed:17241449};
CC Vmax=16.0 nmol/sec/mg enzyme with benzyl alcohol as substrate (in the
CC presence of acetyl CoA and at pH 7.5) {ECO:0000269|PubMed:17241449};
CC Vmax=22.1 nmol/sec/mg enzyme with acetyl CoA as substrate (in the
CC presence of benzyl alcohol and at pH 7.5)
CC {ECO:0000269|PubMed:17241449};
CC Vmax=17.8 nmol/sec/mg enzyme with 2-phenyl ethanol as substrate (in
CC the presence of acetyl CoA and at pH 7.5)
CC {ECO:0000269|PubMed:17241449};
CC Vmax=18.3 nmol/sec/mg enzyme with acetyl CoA as substrate (in the
CC presence of 2-phenyl ethanol and at pH 7.5)
CC {ECO:0000269|PubMed:17241449};
CC Note=kcat is 2.05 sec(-1) with coniferyl alcohol as substrate (in the
CC presence of acetyl CoA and at pH 6) (PubMed:17241449). kcat is 2.32
CC sec(-1) with acetyl CoA as substrate (in the presence of coniferyl
CC alcohol and at pH 6) (PubMed:17241449). kcat is 0.81 sec(-1) with
CC coniferyl alcohol as substrate (in the presence of acetyl CoA and at
CC pH 7.5) (PubMed:17241449). kcat is 1.51 sec(-1) with acetyl CoA as
CC substrate (in the presence of coniferyl alcohol and at pH 7.5)
CC (PubMed:17241449). kcat is 0.82 sec(-1) with benzyl alcohol as
CC substrate (in the presence of acetyl CoA and at pH 7.5)
CC (PubMed:17241449). kcat is 1.13 sec(-1) with acetyl CoA as substrate
CC (in the presence of benzyl alcohol and at pH 7.5) (PubMed:17241449).
CC kcat is 0.91 sec(-1) with 2-phenyl ethanol as substrate (in the
CC presence of acetyl CoA and at pH 7.5) (PubMed:17241449). kcat is 0.93
CC sec(-1) with acetyl CoA as substrate (in the presence of 2-phenyl
CC ethanol and at pH 7.5) (PubMed:17241449).
CC {ECO:0000269|PubMed:17241449};
CC pH dependence:
CC Optimum pH is 6. Larger substrate spectrum at pH 7.5, with a lower
CC activity, thought. {ECO:0000269|PubMed:17241449};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:17241449}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6TXD2}.
CC -!- TISSUE SPECIFICITY: Confined to flowers, mostly in petals limbs.
CC {ECO:0000269|PubMed:17241449, ECO:0000269|PubMed:20543029}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels early stages of floral
CC development (e.g. small bud, medium bud and tube expansion), but
CC accumulates at higher levels at later stages of flower development
CC (e.g. anthesis and 2 days post-anthesis) (PubMed:17241449,
CC PubMed:20543029). Following fertilization by pollen (pollination), a
CC rapid ethylene biosynthesis in the stigma, style and ovary, and later
CC in the corolla, lead to a reduced expression and a subsequent decrease
CC of volatile emission (PubMed:17241449). {ECO:0000269|PubMed:17241449,
CC ECO:0000269|PubMed:20543029}.
CC -!- INDUCTION: Up-regulated by EOBII (PubMed:20543029). Circadian-
CC regulation with peak levels occurring at the end of the light period
CC and during the night in flowers (PubMed:17241449, PubMed:26124104).
CC Repressed by ethylene, especially following pollination
CC (PubMed:17241449). {ECO:0000269|PubMed:17241449,
CC ECO:0000269|PubMed:20543029, ECO:0000269|PubMed:26124104}.
CC -!- DISRUPTION PHENOTYPE: Suppression of isoeugenol biosynthesis and
CC reduction of several floral volatiles including phenylacetaldehyde,
CC phenylethyl alcohol, phenyl-ethyl acetate, phenylethyl benzoate and
CC benzyl acetate, but increased accumulation of homovanillic acid and
CC coniferyl aldehyde. {ECO:0000269|PubMed:17241449}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; DQ767969; ABG75942.1; -; mRNA.
DR AlphaFoldDB; A1XWY7; -.
DR SMR; A1XWY7; -.
DR KEGG; ag:ABG75942; -.
DR BioCyc; MetaCyc:MON-13831; -.
DR BRENDA; 2.3.1.84; 4700.
DR UniPathway; UPA00711; -.
DR GO; GO:0102387; F:2-phenylethanol acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102720; F:acetyl-coenzyme A:acetyl alcohol acetyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0034318; F:alcohol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009723; P:response to ethylene; IEP:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Phenylpropanoid metabolism; Transferase.
FT CHAIN 1..454
FT /note="Coniferyl alcohol acyltransferase"
FT /id="PRO_0000451507"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9FI78"
FT ACT_SITE 384
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9FI78"
SQ SEQUENCE 454 AA; 51120 MW; 1CF632D5753C1D32 CRC64;
MGNTDFHVTV KKKEVVAAVL PMHHEHWLPM SNLDLLLPPL DFGVFFCYKR SKINNDTKDD
DETIKKALAE TLVSFYALAG EVVFNSLGEP ELLCNNRGVD FFHAYADIEL NNLDLYHPDV
SVHEKLIPIK KHGVLSVQVT GLKCGGIVVG CTFDHRVADA YSANMFLVAW AAIARKDNNI
NTVIPSFRRS LLNPRRPPQF DDSFIDSTYV FLSSPPKQPN DVLTSRVYYI NSQEINLLQS
QATRNGSKRS KLECFSAFLW KTIAEGGIDD SKRCKLGIVV DGRQRLRHDS STTMKNYFGN
VLSVPYTEAS VGQLKQTPLG KVADLVHTCL DNVANEHHFP SLIDWVELHR PRQAIVKVYC
KDECNDEAAI VVSSGLRFPL SQVNFGWGCP DFGSYIFPWG GQTGYVMPMP SPNKNGDWIV
YMHLQKKHLD LVETRAPHIF HPLTACYLDL TATY
