BEBT1_PETHY
ID BEBT1_PETHY Reviewed; 460 AA.
AC Q6E593;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Benzyl alcohol O-benzoyltransferase {ECO:0000303|PubMed:15286288};
DE Short=PhBEBT1 {ECO:0000303|PubMed:15286288};
DE EC=2.3.1.196 {ECO:0000269|PubMed:15286288};
DE AltName: Full=Acetyl CoA:3-hydroxybenzyl alcohol acetyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15286288};
DE AltName: Full=Acetyl CoA:benzyl alcohol acetyltransferase {ECO:0000305};
DE EC=2.3.1.224 {ECO:0000269|PubMed:15286288};
DE AltName: Full=Acetyl CoA:geraniol acetyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15286288};
DE AltName: Full=Benzoyl coenzyme A:benzyl alcohol benzoyl transferase {ECO:0000303|PubMed:15286288};
DE Short=Benzyl CoA:benzyl alcohol/phenylethanol benzoyltransferase {ECO:0000303|PubMed:17194766};
DE Short=PhBPBT {ECO:0000303|PubMed:17194766};
DE AltName: Full=Benzyl CoA:(3Z)-hex-3-en-1-ol benzoyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15286288};
DE AltName: Full=Benzyl CoA:2-phenylethanol benzoyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15286288};
DE AltName: Full=Benzyl CoA:3-hydroxybenzyl alcohol benzoyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15286288};
DE AltName: Full=Benzyl CoA:butanol benzoyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15286288};
DE AltName: Full=Benzyl CoA:geraniol benzoyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15286288};
DE AltName: Full=Benzyl CoA:octan-1-ol benzoyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:15286288};
GN Name=BEBT1 {ECO:0000303|PubMed:15286288};
GN Synonyms=BPBT {ECO:0000303|PubMed:17194766};
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, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=cv. Mitchell; TISSUE=Corolla;
RX PubMed=15286288; DOI=10.1104/pp.104.045468;
RA Boatright J., Negre F., Chen X., Kish C.M., Wood B., Peel G., Orlova I.,
RA Gang D., Rhodes D., Dudareva N.;
RT "Understanding in vivo benzenoid metabolism in petunia petal tissue.";
RL Plant Physiol. 135:1993-2011(2004).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Mitchell;
RX PubMed=17194766; DOI=10.1105/tpc.106.046227;
RA Orlova I., Marshall-Colon A., Schnepp J., Wood B., Varbanova M.,
RA Fridman E., Blakeslee J.J., Peer W.A., Murphy A.S., Rhodes D.,
RA Pichersky E., Dudareva N.;
RT "Reduction of benzenoid synthesis in petunia flowers reveals multiple
RT pathways to benzoic acid and enhancement in auxin transport.";
RL Plant Cell 18:3458-3475(2006).
RN [3]
RP 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20070567; DOI=10.1111/j.1365-313x.2010.04127.x;
RA Colon A.M., Sengupta N., Rhodes D., Dudareva N., Morgan J.;
RT "A kinetic model describes metabolic response to perturbations and
RT distribution of flux control in the benzenoid network of Petunia hybrida.";
RL Plant J. 62:64-76(2010).
CC -!- FUNCTION: Involved in the production of volatile organic compounds
CC (VOCs), including floral volatile benzenoids and phenylpropanoids
CC (FVBP), in flowers of fragrant cultivars (e.g. cv. Mitchell and cv.
CC V26), scent attracting pollinators (e.g. the night-active hawkmoth
CC pollinator Manduca sexta) (PubMed:15286288, PubMed:20070567).
CC Acyltransferase that catalyzes the transfer of benzoyl and acetyl
CC moieties to a large variety of potential substrate alcohols, and
CC involved in the formation of volatile esters benzyl benzoate and
CC phenylethyl benzoate from benzoyl-CoA (PubMed:15286288,
CC PubMed:17194766, PubMed:20070567). With acetyl-CoA, mainly active on
CC benzyl alcohol, and, to a lower extent, on 3-hydroxybenzyl alcohol,
CC geraniol, and 2-phenylethanol, but barely active on butanol, 1-octanol,
CC 4-hydroxy-benzyl alcohol, 2-hexanol, cis-3-hexen-1-ol and linalool
CC (PubMed:15286288). With benzoyl-CoA, mainly active on benzyl alcohol,
CC but also efficient on several substrates, including 3-hydroxybenzyl
CC alcohol, 2-phenylethanol, geraniol, butanol, cis-3-hexen-1-ol and 1-
CC octanol (PubMed:15286288). {ECO:0000269|PubMed:15286288,
CC ECO:0000269|PubMed:17194766, ECO:0000269|PubMed:20070567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + benzyl alcohol = benzyl benzoate + CoA;
CC Xref=Rhea:RHEA:30411, ChEBI:CHEBI:17987, ChEBI:CHEBI:41237,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57369; EC=2.3.1.196;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30412;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + benzyl alcohol = benzyl acetate + CoA;
CC Xref=Rhea:RHEA:36147, ChEBI:CHEBI:17987, ChEBI:CHEBI:52051,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.224;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36148;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybenzyl alcohol + acetyl-CoA = 3-hydroxy-benzyl
CC acetate + CoA; Xref=Rhea:RHEA:64828, ChEBI:CHEBI:17069,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:156232;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64829;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxybenzyl alcohol + benzoyl-CoA = 3-hydroxy-benzyl
CC benzoate + CoA; Xref=Rhea:RHEA:64832, ChEBI:CHEBI:17069,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57369, ChEBI:CHEBI:156231;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64833;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-phenylethanol + benzoyl-CoA = CoA + phenethyl benzoate;
CC Xref=Rhea:RHEA:64840, ChEBI:CHEBI:49000, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:156233;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64841;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3Z)-hex-3-en-1-ol + benzoyl-CoA = (3Z)-hex-3-en-1-yl benzoate
CC + CoA; Xref=Rhea:RHEA:64848, ChEBI:CHEBI:28857, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:156235;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64849;
CC Evidence={ECO:0000269|PubMed:15286288};
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:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64625;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + butan-1-ol = butyl benzoate + CoA;
CC Xref=Rhea:RHEA:64636, ChEBI:CHEBI:28885, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:156070;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64637;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geraniol + benzoyl-CoA = (2E)-geranyl benzoate + CoA;
CC Xref=Rhea:RHEA:64844, ChEBI:CHEBI:17447, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:156234;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64845;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + octan-1-ol = CoA + octyl benzoate;
CC Xref=Rhea:RHEA:64852, ChEBI:CHEBI:16188, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:156236;
CC Evidence={ECO:0000269|PubMed:15286288};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64853;
CC Evidence={ECO:0000269|PubMed:15286288};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=682 uM for acetyl-CoA {ECO:0000269|PubMed:15286288};
CC KM=1555 uM for benzoyl-CoA (in the presence of benzyl alcohol)
CC {ECO:0000269|PubMed:15286288};
CC KM=875 uM for benzoyl-CoA (in the presence of phenyl alcohol)
CC {ECO:0000269|PubMed:15286288};
CC KM=28.6 uM for benzyl alcohol (in the presence of acetyl-CoA)
CC {ECO:0000269|PubMed:15286288};
CC KM=444 uM for benzyl alcohol (in the presence of benzoyl-CoA)
CC {ECO:0000269|PubMed:15286288};
CC KM=686 uM for phenyl ethanol (in the presence of benzoyl-CoA)
CC {ECO:0000269|PubMed:15286288};
CC Vmax=15 nmol/sec/mg enzyme with acetyl-CoA as substrate
CC {ECO:0000269|PubMed:15286288};
CC Vmax=194 nmol/sec/mg enzyme with benzoyl-CoA as substrate (in the
CC presence of benzyl alcohol) {ECO:0000269|PubMed:15286288};
CC Vmax=279 nmol/sec/mg enzyme with benzoyl-CoA as substrate (in the
CC presence of phenyl alcohol) {ECO:0000269|PubMed:15286288};
CC Vmax=5.52 nmol/sec/mg enzyme with benzyl alcohol as substrate (in the
CC presence of acetyl-CoA) {ECO:0000269|PubMed:15286288};
CC Vmax=125.5 nmol/sec/mg enzyme with benzyl alcohol as substrate (in
CC the presence of benzoyl-CoA) {ECO:0000269|PubMed:15286288};
CC Vmax=122.9 nmol/sec/mg enzyme with phenyl ethanol as substrate (in
CC the presence of benzoyl-CoA) {ECO:0000269|PubMed:15286288};
CC Note=kcat is 4.4 sec(-1) with acetyl-CoA as substrate
CC (PubMed:15286288). kcat is 57.1 sec(-1) with benzoyl-CoA as substrate
CC (in the presence of benzyl alcohol) (PubMed:15286288). kcat is 81.3
CC sec(-1) with benzoyl-CoA as substrate (in the presence of phenyl
CC alcohol) (PubMed:15286288). kcat is 1.61 sec(-1) with benzyl alcohol
CC as substrate (in the presence of acetyl-CoA) (PubMed:15286288). kcat
CC is 36.9 sec(-1) with benzyl alcohol as substrate (in the presence of
CC benzoyl-CoA) (PubMed:15286288). kcat is 35.8 sec(-1) with phenyl
CC ethanol as substrate (in the presence of benzoyl-CoA)
CC (PubMed:15286288). {ECO:0000269|PubMed:15286288};
CC -!- PATHWAY: Aromatic compound metabolism; benzoyl-CoA degradation.
CC {ECO:0000269|PubMed:15286288}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in flowers, mainly in the
CC limb of flowers corollas, and, at low levels, in roots, stems, sepals
CC and leaves. {ECO:0000269|PubMed:15286288, ECO:0000269|PubMed:17194766,
CC ECO:0000269|PubMed:20543029}.
CC -!- DEVELOPMENTAL STAGE: In corollas, accumulates progressively during
CC flower development, from buds to anthesis, but fades out in senescing
CC flowers. {ECO:0000269|PubMed:15286288, ECO:0000269|PubMed:20543029}.
CC -!- INDUCTION: Circadian-regulation with peak levels occurring during the
CC night period (11 pm) in flowers. {ECO:0000269|PubMed:15286288}.
CC -!- DISRUPTION PHENOTYPE: Decreased endogenous pool of benzoic acid
CC (BA)/benzylbenzoate and lower methylbenzoate emission, but increased
CC emission of benzyl alcohol and benzylaldehyde (PubMed:17194766,
CC PubMed:20070567). Increase in the flux from cinnamic acid (CA) to
CC coumaric acid and to flavonoids (PubMed:17194766). Delayed flowering
CC time, large flowers and anthers, delayed anthesis, as well as large and
CC dark seeds accumulating abnormal high levels of flavonoids and
CC anthocyanins (PubMed:17194766). Greater internode length and stem
CC diameter associated with an increased lignin accumulation
CC (PubMed:17194766). Fewer first-order lateral branches but longer
CC primary roots (PubMed:17194766). Seedlings exhibit epinastic cotyledons
CC with fused or supernumerary cotyledons (PubMed:17194766). Increased
CC auxin flux in roots (PubMed:17194766). {ECO:0000269|PubMed:17194766,
CC ECO:0000269|PubMed:20070567}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; AY563157; AAT68601.1; -; mRNA.
DR EMBL; AY611496; AAU06226.1; -; mRNA.
DR AlphaFoldDB; Q6E593; -.
DR SMR; Q6E593; -.
DR KEGG; ag:AAU06226; -.
DR BRENDA; 2.3.1.196; 4700.
DR UniPathway; UPA00739; -.
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:0006084; P:acetyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:1901787; P:benzoyl-CoA metabolic process; IDA:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Transferase.
FT CHAIN 1..460
FT /note="Benzyl alcohol O-benzoyltransferase"
FT /id="PRO_0000451508"
FT ACT_SITE 167
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 460 AA; 51042 MW; 04DF83A363A29D8B CRC64;
MDSKQSSELV FTVRRQEPEL IAPAKPTPRE TKFLSDIDDQ EGLRFQIPVI NFYRKDSSMG
GKDPVEVIKK AIAETLVFYY PFAGRLREGN DRKLMVDCTG EGVMFVEANA DVTLEEFGDE
LQPPFPCLEE LLYDVPGSAG VLHCPLLLIQ VTRLRCGGFI FALRLNHTMS DAPGLVQFMT
AVGEMARGAT APSTLPVWCR ELLNARNPPQ VTCTHHEYEE VPDTKGTLIP LDDMVHRSFF
FGPTEVSALR RFVPPHLHNC STFEVLTAAL WRCRTISIKP DPEEEVRVLC IVNARSRFNP
QLPSGYYGNA FAFPVAVTTA EKLCKNPLGY ALELVKKTKS DVTEEYMKSV ADLMVIKGRP
HFTVVRTYLV SDVTRAGFGE VDFGWGKAVY GGPAKGGVGA IPGVASFYIP FRNKKGENGI
VVPICLPGFA MEKFVKELDS MLKGDAQLDN KKYAFITPAL
