ID   BEATH_CLABR             Reviewed;         433 AA.
AC   O64988;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Acetyl-CoA-benzylalcohol acetyltransferase;
DE            Short=CbBEAT-1;
DE            EC=2.3.1.224;
GN   Name=BEAT;
OS   Clarkia breweri (Fairy fans) (Eucharidium breweri).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX   NCBI_TaxID=36903;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 189-210; 279-306 AND
RP   343-379, FUNCTION, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. scented line;
RX   PubMed=9628024; DOI=10.1046/j.1365-313x.1998.00121.x;
RA   Dudareva N., D'Auria J.C., Nam K.H., Raguso R.A., Pichersky E.;
RT   "Acetyl-CoA:benzylalcohol acetyltransferase--an enzyme involved in floral
RT   scent production in Clarkia breweri.";
RL   Plant J. 14:297-304(1998).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. scented line;
RX   PubMed=10588064; DOI=10.1093/oxfordjournals.pcp.a029623;
RA   Nam K.H., Dudareva N., Pichersky E.;
RT   "Characterization of benzylalcohol acetyltransferases in scented and non-
RT   scented Clarkia species.";
RL   Plant Cell Physiol. 40:916-923(1999).
CC   -!- FUNCTION: Involved in the biosynthesis of benzyl acetate, a major
CC       constituent of the floral scent. Can use benzylalcohol,
CC       cinnamylalcohol, 3-cis-hexene-1-ol or heptanol as substrates. Has some
CC       activity with 2-phenylethanol and 2-naphtalene-ethanol, but no activity
CC       with linalool, 2-hydroxybenzylalcohol, 3-hydroxybenzylalcohol or 4-
CC       hydroxybenzylalcohol. {ECO:0000269|PubMed:10588064,
CC       ECO:0000269|PubMed:9628024}.
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   -!- 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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=240 uM for benzyl alcohol {ECO:0000269|PubMed:10588064};
CC         KM=24 uM for acetyl-CoA {ECO:0000269|PubMed:10588064};
CC         Vmax=556 pmol/sec/mg enzyme {ECO:0000269|PubMed:10588064};
CC   -!- TISSUE SPECIFICITY: Expressed in petals, style, sepals and stamens.
CC       Very low expression in stigma and not detected in leaves.
CC       {ECO:0000269|PubMed:9628024}.
CC   -!- DEVELOPMENTAL STAGE: Expression in petals peaks on the day of anthesis.
CC       {ECO:0000269|PubMed:10588064, ECO:0000269|PubMed:9628024}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC   -!- CAUTION: The cv. non-scented line contains a lower amount of the
CC       protein (AC Q9SPU3) and a lower activity, even though it has similar
CC       levels of mRNA (PubMed:10588064). {ECO:0000305|PubMed:10588064}.
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DR   EMBL; AF043464; AAC18062.1; -; mRNA.
DR   AlphaFoldDB; O64988; -.
DR   SMR; O64988; -.
DR   KEGG; ag:AAC18062; -.
DR   BRENDA; 2.3.1.224; 1437.
DR   SABIO-RK; O64988; -.
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   Gene3D; 3.30.559.10; -; 2.
DR   InterPro; IPR023213; CAT-like_dom_sf.
PE   1: Evidence at protein level;
KW   Acyltransferase; Direct protein sequencing; Transferase.
FT   CHAIN           1..433
FT                   /note="Acetyl-CoA-benzylalcohol acetyltransferase"
FT                   /id="PRO_0000424078"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        377
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   433 AA;  48198 MW;  2E8D68D56EBE574C CRC64;
     MNVTMHSKKL LKPSIPTPNH LQKLNLSLLD QIQIPFYVGL IFHYETLSDN SDITLSKLES
     SLSETLTLYY HVAGRYNGTD CVIECNDQGI GYVETAFDVE LHQFLLGEES NNLDLLVGLS
     GFLSETETPP LAAIQLNMFK CGGLVIGAQF NHIIGDMFTM STFMNSWAKA CRVGIKEVAH
     PTFGLAPLMP SAKVLNIPPP PSFEGVKFVS KRFVFNENAI TRLRKEATEE DGDGDDDQKK
     KRPSRVDLVT AFLSKSLIEM DCAKKEQTKS RPSLMVHMMN LRKRTKLALE NDVSGNFFIV
     VNAESKITVA PKITDLTESL GSACGEIISE VAKVDDAEVV SSMVLNSVRE FYYEWGKGEK
     NVFLYTSWCR FPLYEVDFGW GIPSLVDTTA VPFGLIVLMD EAPAGDGIAV RACLSEHDMI
     QFQQHHQLLS YVS