ID   AT9_ACTDE               Reviewed;         432 AA.
AC   P0DO25;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   02-DEC-2020, sequence version 1.
DT   03-AUG-2022, entry version 7.
DE   RecName: Full=Alcohol acyltransferase 9 {ECO:0000303|PubMed:21450321};
DE            Short=AdAT9 {ECO:0000303|PubMed:21450321};
DE            EC=2.3.1.268 {ECO:0000269|PubMed:21450321};
GN   Name=AT9 {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].
RC   TISSUE=Fruit;
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   [2]
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 acetyl-CoA:alcohol O-acyltransferase
CC       activity (PubMed:21450321). {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   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ethanol = CoA + ethyl acetate;
CC         Xref=Rhea:RHEA:55972, ChEBI:CHEBI:16236, ChEBI:CHEBI:27750,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.268;
CC         Evidence={ECO:0000269|PubMed:21450321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55973;
CC         Evidence={ECO:0000269|PubMed:21450321};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + butan-1-ol = butyl acetate + CoA;
CC         Xref=Rhea:RHEA:64632, ChEBI:CHEBI:28885, ChEBI:CHEBI:31328,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
CC         Evidence={ECO:0000269|PubMed:21450321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64633;
CC         Evidence={ECO:0000269|PubMed:21450321};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butan-1-ol + propanoyl-CoA = butyl propanoate + CoA;
CC         Xref=Rhea:RHEA:64644, ChEBI:CHEBI:28885, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57392, ChEBI:CHEBI:89831;
CC         Evidence={ECO:0000269|PubMed:21450321};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64645;
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; HO772635; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P0DO25; -.
DR   SMR; P0DO25; -.
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..432
FT                   /note="Alcohol acyltransferase 9"
FT                   /id="PRO_0000451703"
FT   ACT_SITE        156
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FI78"
FT   ACT_SITE        379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FI78"
SQ   SEQUENCE   432 AA;  47716 MW;  CE616A5ECDE2AFE5 CRC64;
     MASSVRLVKK PVLVAPVDPT PSTVLSLSSL DSQLFLRFPI EYLLVYASPH GVDRAVTAAR
     VKAALARSLV PYYPLAGRVK TRPDSTGLDV VCQAQGAGLL EAVSDYTASD FQRAPRSVTE
     WRKLLLVEVF KVVPPLVVQL TWLSDGCVAL GVGFSHCVID GIGSSEFLNL FAELATGRAR
     LSEFQPKPVW DRHLLNSAGR TNLGTHPEFG RVPDLSGFVT RFTQERLSPT SITFDKTWLK
     ELKNIAMSTS QPGEFPYTSF EVLSGHIWRS WARSLNLPAK QVLKLLFSIN IRNRVKPSLP
     AGYYGNAFVL GCAQTSVKDL TEKGLGYCAD LVRGAKERVG DEYAREVVES VSWPRRASPD
     SVGVLIISQW SRLGLDRVDF GLGRPVQVGP ICCDRYCLFL PVRDRTESVK VMVAVPTSAV
     DRYEYFIRSP YS