ATGSA_MALDO
ID ATGSA_MALDO Reviewed; 459 AA.
AC A0A498KFL4; V9P9T8;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-JUN-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=Alcohol acyl transferase 1 allele GSa {ECO:0000303|PubMed:24661745};
DE Short=AAT1-GSa {ECO:0000303|PubMed:24661745};
DE EC=2.3.1.- {ECO:0000269|PubMed:24661745};
GN Name=AAT1GSA {ECO:0000303|PubMed:24661745};
GN ORFNames=DVH24_026095 {ECO:0000312|EMBL:RXI06959.1};
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Granny Smith;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1; TISSUE=Leaf;
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of volatile esters which confer
CC ripe apple fruit flavor (PubMed:24661745). Alcohol acyl transferase
CC that can use a wide range of alcohols as substrate, including 2-
CC methylbutanol, hexanol and ethanol, to produce esters such as butyl
CC butanoate, butyl hexanoate, hexyl butanoate, ethyl butanoate and ethyl
CC hexanoate and, to some extent, 2-methylbutyl acetate (2MBA), butyl
CC acetate, hexyl acetate and 2-methylbutyl butanoate (2MBB)
CC (PubMed:24661745). {ECO:0000269|PubMed:24661745}.
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:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64633;
CC Evidence={ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butan-1-ol + butanoyl-CoA = butyl butanoate + CoA;
CC Xref=Rhea:RHEA:65400, ChEBI:CHEBI:28885, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:87429;
CC Evidence={ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65401;
CC Evidence={ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butan-1-ol + hexanoyl-CoA = butyl hexanoate + CoA;
CC Xref=Rhea:RHEA:65404, ChEBI:CHEBI:28885, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:89561;
CC Evidence={ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65405;
CC Evidence={ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + hexan-1-ol = CoA + hexyl butanoate;
CC Xref=Rhea:RHEA:65444, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:87393, ChEBI:CHEBI:87559;
CC Evidence={ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65445;
CC Evidence={ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + hexan-1-ol = CoA + hexyl acetate;
CC Xref=Rhea:RHEA:65460, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:87393, ChEBI:CHEBI:87510;
CC Evidence={ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65461;
CC Evidence={ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutan-1-ol + butanoyl-CoA = 2-methylbutyl butanoate +
CC CoA; Xref=Rhea:RHEA:65464, ChEBI:CHEBI:48945, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:156490;
CC Evidence={ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65465;
CC Evidence={ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + ethanol = CoA + ethyl butanoate;
CC Xref=Rhea:RHEA:65448, ChEBI:CHEBI:16236, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57371, ChEBI:CHEBI:88764;
CC Evidence={ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65449;
CC Evidence={ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + hexanoyl-CoA = CoA + ethyl hexanoate;
CC Xref=Rhea:RHEA:65452, ChEBI:CHEBI:16236, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:86055;
CC Evidence={ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65453;
CC Evidence={ECO:0000269|PubMed:24661745};
CC -!- TISSUE SPECIFICITY: Highly expressed in the cortex and skin of ripe
CC fruit. {ECO:0000269|PubMed:24661745}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively during fruit
CC development, but fades out in ripe fruit.
CC {ECO:0000269|PubMed:24661745}.
CC -!- MISCELLANEOUS: The fruit of cv. Royal Gala exhibits a high ester
CC accumulation, whereas the cv. Granny Smith contains low ester levels;
CC this influences strongly the ripe apple fruit aroma.
CC {ECO:0000305|PubMed:24661745}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The intimacy of flavour
CC - Issue 231 of December 2020;
CC URL="https://web.expasy.org/spotlight/back_issues/231/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KC291132; AGW30203.1; -; Genomic_DNA.
DR EMBL; RDQH01000328; RXI06959.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498KFL4; -.
DR SMR; A0A498KFL4; -.
DR STRING; 3750.XP_008343918.1; -.
DR Proteomes; UP000290289; Chromosome 2.
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 Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..459
FT /note="Alcohol acyl transferase 1 allele GSa"
FT /id="PRO_0000451711"
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 VARIANT 454..459
FT /note="RIMSMM -> SQ (in strain: cv. Granny Smith)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 51206 MW; FD75BF461AFB648F CRC64;
MMPLAVLHVK RLQPELITPA KPTPQETKFL SDIDDQEFLR FQVPIIMCYK DNPSLNKNRN
PVKVIREALS RALVYYYPLA GRLREGPNRK LVVDCNGEGI LFIEASADVT LEQLGDKILP
PCPLLEEFLF NFPGSDGIIG CPLVLVQVTC LTCGGFILAL RLNHTMCDAA GLLLFLTAIA
EMARGAHAPS ILPVWERELL FARDPPRITC AHHEYEDVIG HSDGSYASSN QSNMVQRSFY
FGAKEMRVLR KQIPPHLIST CSTFDLITAC LWKCRTLALN INPKEAVRVS CIVNARGKHN
NVRLPLGYYG NAFAFPAAIS KAEPLCKNPL GYALELVKKA KATMNEEYLR SVADLLVLRG
RPQYSSTGSY LIVSDNTRAG FGDVNFGWGQ PVFAGPVKAL DLISFYVQHK NNAEDGILVP
MCLPSSAMER FQQELERITQ EPKEDICNNL RSTRIMSMM
