ID   AAT2_MALDO              Reviewed;         459 AA.
AC   Q6R311; B2ZZ12;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Alcohol acyl transferase 2 {ECO:0000303|PubMed:16524607};
DE            Short=MdAAT2 {ECO:0000303|PubMed:16524607};
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q64FJ6};
GN   Name=AAT2 {ECO:0000303|PubMed:16524607};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Golden Delicious;
RX   PubMed=16524607; DOI=10.1016/j.phytochem.2006.01.027;
RA   Li D., Xu Y., Xu G., Gu L., Li D., Shu H.;
RT   "Molecular cloning and expression of a gene encoding alcohol
RT   acyltransferase (MdAAT2) from apple (cv. Golden Delicious).";
RL   Phytochemistry 67:658-667(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 227-362, FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND INDUCTION BY ETHYLENE.
RC   STRAIN=cv. Tsugaru; TISSUE=Fruit cortical tissue;
RX   AGRICOLA=IND44252665; DOI=10.1016/j.foodchem.2009.04.109;
RA   Ban Y., Oyama-Okubo N., Honda C., Nakayama M., Moriguchi T.;
RT   "Emitted and endogenous volatiles in 'Tsugaru' apple: The mechanism of
RT   ester and (E,E)-alpha-farnesene accumulation.";
RL   Food Chem. 118:272-277(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of volatile esters which confer
CC       ripe apple fruit flavor (Ref.2). Alcohol acyl transferase that can use
CC       a wide range of alcohols as substrate to produce esters (By
CC       similarity). {ECO:0000250|UniProtKB:Q64FJ6, ECO:0000269|Ref.2}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the cortex and skin of ripe
CC       fruit. {ECO:0000269|Ref.2}.
CC   -!- DEVELOPMENTAL STAGE: Accumulates progressively during fruit
CC       development. {ECO:0000269|Ref.2}.
CC   -!- INDUCTION: Slightly induced by ethylene. {ECO:0000269|Ref.2}.
CC   -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR   EMBL; AY517491; AAS79797.1; -; mRNA.
DR   EMBL; AB370229; BAG48171.1; -; mRNA.
DR   AlphaFoldDB; Q6R311; -.
DR   SMR; Q6R311; -.
DR   GO; GO:0016746; F:acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0006066; P:alcohol metabolic process; ISS: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   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           1..459
FT                   /note="Alcohol acyl transferase 2"
FT                   /id="PRO_0000451707"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FI78"
FT   ACT_SITE        385
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FI78"
FT   CONFLICT        269
FT                   /note="A -> T (in Ref. 2; BAG48171)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   459 AA;  51210 MW;  C1F4DAA50C44D783 CRC64;
     MMPFSVLQVK RLQLELITPA KPTLQEAKFL SDIDDQEGLR FQVPVIMCYK DNPSLNKNCN
     PVKVIREALS RALVYYYPLA GRLKEGPNRK LMVDCNGEGI LFVEASADVT LEQLGDKILP
     PCPLLEEFLF NFPGSDGIIG CPLLLVQVTC LTCGGFILAL RVNHTMCDAP GLLLFLTAIA
     EMARGAHAPS ILPVWERELL FSRDPPRITC AHHEYEDVID HSDGLYASSN QSNMVQRSFY
     FGAKEMRVLR KQIPPHLIST CSTFDLITAC LWKCRTLALN INPKEAVRVS CIVNARGKHN
     NVRLPLGYYG NAFAFPAAIS KAEPLCKNPL GYALELVKKA KATMNEEYLR SVADLLVLRG
     RPQYSSTGSY LIVSDNTRAG FGDVNFGWGQ PVFAGPAKAL DLISFYVQHK NNTEDGILVP
     MCLPSSAMER FQQELERITQ EPKEDICNNL RSTRIMSMM