BEATL_CLABR
ID BEATL_CLABR Reviewed; 433 AA.
AC Q9SPU3;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Acetyl-CoA-benzylalcohol acetyltransferase;
DE Short=CbBEAT-2;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. non-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.
CC {ECO:0000269|PubMed:10588064}.
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:10588064};
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:10588064};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=120 uM for benzylalcohol {ECO:0000269|PubMed:10588064};
CC Vmax=683 pmol/sec/mg enzyme {ECO:0000269|PubMed:10588064};
CC -!- DEVELOPMENTAL STAGE: Expression in petals peaks on the day of anthesis.
CC {ECO:0000269|PubMed:10588064}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC -!- CAUTION: The cv. scented line contains a higher amount of the protein
CC (AC O64988) and a higher activity, even though it has similar levels of
CC mRNA (PubMed:10588064). {ECO:0000305|PubMed:10588064}.
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DR EMBL; AF139130; AAF04787.1; -; mRNA.
DR AlphaFoldDB; Q9SPU3; -.
DR SMR; Q9SPU3; -.
DR SABIO-RK; Q9SPU3; -.
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; Transferase.
FT CHAIN 1..433
FT /note="Acetyl-CoA-benzylalcohol acetyltransferase"
FT /id="PRO_0000424079"
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; 48195 MW; 905C6B39F35494D0 CRC64;
MNVTMHSKKL LKPSIPTPNH LQKLNLSLLD QIQIPFYVGL IFHYETLSDN SDITLSKLES
SLSETLTLYY HVAGRYNGTD CVIECNDQGI GYVETAFDVE LHQFLLGEES NNLDLLVGLS
GFLSETETPP LAAIQLNMFK CGGLVIGAQF NHIIGDMFTM STFMNSWAKA CRVGIKEVAH
PTFGLAPLMP SAKVLNIPPP PSFEGVKFVS KRFVFHENAL TRLRKEATEE DGDGDDDQKK
KRPSRVDLVT AFLSKSLIEM DCAPKELTKS RPSLMVHMMN LRKRTKLALE NDVSGNFFIV
VNAESKITVA PKITDLTESL GSACGEIISE VAKVDDAEVV SSMVLNSVRE FYYEWGKGEK
NVFVYSSWCR FPLYEVDFGW GIPSLVDTTA FPFGLIVLMD EAPAGDGIAV RACLSEHDMI
QFQQHHQLLS YVS