AT1_ACTDE
ID AT1_ACTDE Reviewed; 456 AA.
AC A0A068BGA5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Alcohol acyltransferase 1 {ECO:0000303|PubMed:21450321};
DE Short=AdAT1 {ECO:0000303|PubMed:21450321};
DE EC=2.3.1.- {ECO:0000269|PubMed:21450321};
GN Name=AT1 {ECO:0000303|PubMed:21450321};
OS Actinidia deliciosa (Kiwi).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Actinidiaceae; Actinidia.
OX NCBI_TaxID=3627;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=24661745; DOI=10.1111/tpj.12518;
RA Souleyre E.J.F., Chagne D., Chen X., Tomes S., Turner R.M., Wang M.Y.,
RA Maddumage R., Hunt M.B., Winz R.A., Wiedow C., Hamiaux C., Gardiner S.E.,
RA Rowan D.D., Atkinson R.G.;
RT "The AAT1 locus is critical for the biosynthesis of esters contributing to
RT 'ripe apple' flavour in 'Royal Gala' and 'Granny Smith' apples.";
RL Plant J. 78:903-915(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Petal;
RA Beuning L., Bowen J., Crowhurst R., Gleave A., Janssen B., McArtney S.,
RA Newcomb R., Ross G., Snowden K., Walton E., Yauk Y.;
RT "Plant and food research apple EST project.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP INDUCTION BY ETHYLENE, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21450321; DOI=10.1016/j.phytochem.2011.02.026;
RA Guenther C.S., Chervin C., Marsh K.B., Newcomb R.D., Souleyre E.J.F.;
RT "Characterisation of two alcohol acyltransferases from kiwifruit (Actinidia
RT spp.) reveals distinct substrate preferences.";
RL Phytochemistry 72:700-710(2011).
CC -!- FUNCTION: Involved in the biosynthesis of volatile esters which confer
CC kiwifruit flavor (PubMed:21450321). Alcohol acyl transferase that can
CC use a wide range of alcohols as substrate to produce esters
CC (PubMed:21450321). Exhibits benzoyl-CoA:alcohol O-acyltransferase
CC activity (PubMed:21450321). {ECO:0000269|PubMed:21450321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-(methylsulfanyl)propanoyl-CoA + butan-1-ol = butyl 3-
CC (methylsulfanyl)propanoate + CoA; Xref=Rhea:RHEA:64676,
CC ChEBI:CHEBI:28885, ChEBI:CHEBI:57287, ChEBI:CHEBI:82815,
CC ChEBI:CHEBI:156073; Evidence={ECO:0000269|PubMed:21450321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64677;
CC Evidence={ECO:0000269|PubMed:21450321};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=benzoyl-CoA + ethanol = CoA + ethyl benzoate;
CC Xref=Rhea:RHEA:64680, ChEBI:CHEBI:16236, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57369, ChEBI:CHEBI:156074;
CC Evidence={ECO:0000269|PubMed:21450321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64681;
CC Evidence={ECO:0000269|PubMed:21450321};
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:21450321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64637;
CC Evidence={ECO:0000269|PubMed:21450321};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(methylsulfanyl)acetyl-CoA + butan-1-ol = butyl 2-
CC (methylsulfanyl)acetate + CoA; Xref=Rhea:RHEA:64672,
CC ChEBI:CHEBI:28885, ChEBI:CHEBI:57287, ChEBI:CHEBI:156076,
CC ChEBI:CHEBI:156077; Evidence={ECO:0000269|PubMed:21450321};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64673;
CC Evidence={ECO:0000269|PubMed:21450321};
CC -!- TISSUE SPECIFICITY: Expressed in fruit. {ECO:0000269|PubMed:21450321}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in kiwifruit during ripening.
CC {ECO:0000269|PubMed:21450321}.
CC -!- INDUCTION: Induced by ethylene in ripe fruits.
CC {ECO:0000269|PubMed:21450321}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; KJ626345; AIC83790.1; -; mRNA.
DR EMBL; HO772637; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; A0A068BGA5; -.
DR SMR; A0A068BGA5; -.
DR BioCyc; MetaCyc:MON-16563; -.
DR GO; GO:0016746; F:acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006066; P:alcohol metabolic process; IDA:UniProtKB.
DR GO; GO:0009836; P:fruit ripening, climacteric; IEP: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; Transferase.
FT CHAIN 1..456
FT /note="Alcohol acyltransferase 1"
FT /id="PRO_0000451700"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9FI78"
FT ACT_SITE 382
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9FI78"
SQ SEQUENCE 456 AA; 50972 MW; 10CFCB7D1E89D4C0 CRC64;
MASFPPSLVF TVRRKEPILV LPSKPTPREL KQLSDIDDQE GLRFQVPVIM FYKRKLSTEG
EDPVKVIREA LAEALAFYYP FAGRLIEGPN RKLMVDCTSE GVLFIEADAD IELNQLIGDT
IDPGTYLDEL LHDVPGSEGI LGCPLLLIQV TRFRCGGWAF AIRLNHTMSD TLGLVQFLTT
IAEFTRGAEG APSVPPVWQR EFLAARQPPF IPFQHHEYEQ VIDTTPDDNK KSMTHKSFFF
GPKEIRAIRS HLPLHHRSTS STFDVLTACL WRCRTCALVL DPKKTVRISC AASGRGKHDL
HVPRGYYGNV SAFPATVLRA GMISTSPLEY AMEGVKKAKA RMTGEYLRSV ADLMVTKGRP
LYTVVGNYIV SDMTRVGLDT IDFGWGKPVY GGPARAFPLI SFYGRFKDNK GEDGIVVLIC
LPEAAMKRFQ EELKKMTGEH VDGPFDYKPI KVVSKL
