ATRGA_MALDO
ID ATRGA_MALDO Reviewed; 455 AA.
AC Q64FJ6; B2ZZ12;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Alcohol acyl transferase 1 allele RGa {ECO:0000303|PubMed:24661745};
DE Short=AAT1-RGa {ECO:0000303|PubMed:24661745};
DE Short=MpAAT1 {ECO:0000303|PubMed:15955071};
DE EC=2.3.1.- {ECO:0000269|PubMed:15955071, ECO:0000269|PubMed:24661745};
GN Name=AAT1RGA {ECO:0000303|PubMed:24661745};
GN Synonyms=AAT1 {ECO:0000303|PubMed:15955071};
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=cv. Royal Gala;
RX PubMed=15955071; DOI=10.1111/j.1742-4658.2005.04732.x;
RA Souleyre E.J.F., Greenwood D.R., Friel E.N., Karunairetnam S.,
RA Newcomb R.D.;
RT "An alcohol acyl transferase from apple (cv. Royal Gala), MpAAT1, produces
RT esters involved in apple fruit flavor.";
RL FEBS J. 272:3132-3144(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE,
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, GENE FAMILY,
RP AND NOMENCLATURE.
RC STRAIN=cv. Royal Gala;
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 [3]
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 (PubMed:24661745, Ref.3). Alcohol acyl
CC transferase that can use a wide range of alcohols as substrate,
CC including 2-methylbutanol, hexanol and ethanol, to produce esters such
CC as butyl butanoate, butyl hexanoate, hexyl butanoate, 2-methylbutyl
CC acetate (2MBA), butyl acetate, hexyl acetate and 2-methylbutyl
CC butanoate (2MBB), and, to some extent, ethyl butanoate and ethyl
CC hexanoate (PubMed:24661745, PubMed:15955071).
CC {ECO:0000269|PubMed:15955071, ECO:0000269|PubMed:24661745,
CC ECO:0000269|Ref.3}.
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:15955071, ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64633;
CC Evidence={ECO:0000269|PubMed:15955071, 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:15955071, ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65461;
CC Evidence={ECO:0000269|PubMed:15955071, ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutan-1-ol + acetyl-CoA = 2-methylbutyl acetate + CoA;
CC Xref=Rhea:RHEA:65456, ChEBI:CHEBI:48945, ChEBI:CHEBI:50585,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288;
CC Evidence={ECO:0000269|PubMed:15955071, ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65457;
CC Evidence={ECO:0000269|PubMed:15955071, 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:15955071, ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65445;
CC Evidence={ECO:0000269|PubMed:15955071, ECO:0000269|PubMed:24661745};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexan-1-ol + hexanoyl-CoA = CoA + hexyl hexanoate;
CC Xref=Rhea:RHEA:65484, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:87393, ChEBI:CHEBI:156492;
CC Evidence={ECO:0000269|PubMed:15955071};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65485;
CC Evidence={ECO:0000269|PubMed:15955071};
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:15955071, ECO:0000269|PubMed:24661745};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65465;
CC Evidence={ECO:0000269|PubMed:15955071, 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 + 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 -!- CATALYTIC ACTIVITY:
CC Reaction=hexan-1-ol + octanoyl-CoA = CoA + hexyl octanoate;
CC Xref=Rhea:RHEA:65528, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:87393, ChEBI:CHEBI:87490;
CC Evidence={ECO:0000269|PubMed:15955071};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65529;
CC Evidence={ECO:0000269|PubMed:15955071};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methylbutan-1-ol + hexanoyl-CoA = 2-methylbutyl hexanoate +
CC CoA; Xref=Rhea:RHEA:65532, ChEBI:CHEBI:48945, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:156542;
CC Evidence={ECO:0000269|PubMed:15955071};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65533;
CC Evidence={ECO:0000269|PubMed:15955071};
CC -!- ACTIVITY REGULATION: Repressed by metal ions, zinc ions having the
CC strongest impact, and magnesium, cobalt, nickel, manganese and calcium
CC ions acting as partial inhibitors (PubMed:15955071). Strongly inhibited
CC by p-chloromercuribenzoic acid (PCMB) and, to a lower extent, by
CC dithiothreitol (PubMed:15955071). {ECO:0000269|PubMed:15955071}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for acetyl-CoA (in the presence of butan-1-ol)
CC {ECO:0000269|PubMed:15955071};
CC KM=2.7 mM for acetyl-CoA (in the presence of hexanol)
CC {ECO:0000269|PubMed:15955071};
CC KM=0.09 mM for acetyl-CoA (in the presence of 2-methylbutanol)
CC {ECO:0000269|PubMed:15955071};
CC KM=7.4 mM for hexanol (in the presence of acetyl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=1.5 mM for hexanol (in the presence of butyryl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=2.6 mM for hexanol (in the presence of hexanoyl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=3.1 mM for hexanol (in the presence of octanoyl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=2.7 mM for butan-1-ol (in the presence of acetyl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=12.4 mM for butan-1-ol (in the presence of octanoyl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=1.1 mM for 2-methylbutanol (in the presence of acetyl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=1.7 mM for 2-methylbutanol (in the presence of butyryl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=3.2 mM for 2-methylbutanol (in the presence of hexanoyl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC KM=6.2 mM for 2-methylbutanol (in the presence of octanoyl-CoA)
CC {ECO:0000269|PubMed:15955071};
CC Vmax=20 nmol/min/mg enzyme with acetyl-CoA as substrate (in the
CC presence of butanol) {ECO:0000269|PubMed:15955071};
CC Vmax=376 nmol/min/mg enzyme with acetyl-CoA as substrate (in the
CC presence of hexanol) {ECO:0000269|PubMed:15955071};
CC Vmax=16.6 nmol/min/mg enzyme with acetyl-CoA as substrate (in the
CC presence of 2-methylbutanol) {ECO:0000269|PubMed:15955071};
CC Vmax=148.6 nmol/min/mg enzyme with hexanol as substrate (in the
CC presence of acetyl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=207.6 nmol/min/mg enzyme with hexanol as substrate (in the
CC presence of butyryl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=320 nmol/min/mg enzyme with hexanol as substrate (in the
CC presence of hexanoyl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=252.3 nmol/min/mg enzyme with hexanol as substrate (in the
CC presence of octanoyl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=35.4 nmol/min/mg enzyme with butanol as substrate (in the
CC presence of acetyl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=47.4 nmol/min/mg enzyme with butanol as substrate (in the
CC presence of octanoyl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=66.8 nmol/min/mg enzyme with 2-methylbutanol as substrate (in
CC the presence of acetyl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=41.3 nmol/min/mg enzyme with 2-methylbutanol as substrate (in
CC the presence of butyryl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=47.1 nmol/min/mg enzyme with 2-methylbutanol as substrate (in
CC the presence of hexanoyl-CoA) {ECO:0000269|PubMed:15955071};
CC Vmax=53.7 nmol/min/mg enzyme with 2-methylbutanol as substrate (in
CC the presence of octanoyl-CoA) {ECO:0000269|PubMed:15955071};
CC pH dependence:
CC Optimum pH is 7-9. {ECO:0000269|PubMed:15955071};
CC Temperature dependence:
CC Optimum temperature is 20-37 degrees Celsius.
CC {ECO:0000269|PubMed:15955071};
CC -!- TISSUE SPECIFICITY: Highly expressed in the cortex and skin of ripe
CC fruit. {ECO:0000269|PubMed:24661745, ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: Accumulates progressively during fruit
CC development. {ECO:0000269|PubMed:24661745, ECO:0000269|Ref.3}.
CC -!- INDUCTION: Slightly induced by ethylene. {ECO:0000269|Ref.3}.
CC -!- DISRUPTION PHENOTYPE: Reduction in total esters production but
CC accumulation of precursor alcohols and aldehydes in ripening apple
CC fruits, leading to modified aroma and flavor.
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/";
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DR EMBL; AY707098; AAU14879.2; -; mRNA.
DR EMBL; KC291129; AGW30200.1; -; Genomic_DNA.
DR EMBL; AB370229; BAG48171.1; -; mRNA.
DR RefSeq; NP_001315675.1; NM_001328746.1.
DR RefSeq; XP_008343918.1; XM_008345696.1.
DR AlphaFoldDB; Q64FJ6; -.
DR SMR; Q64FJ6; -.
DR GeneID; 103406706; -.
DR KEGG; mdm:103406706; -.
DR OrthoDB; 1130893at2759; -.
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 Transferase.
FT CHAIN 1..455
FT /note="Alcohol acyl transferase 1 allele RGa"
FT /id="PRO_0000451708"
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. 3; BAG48171)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 455 AA; 50716 MW; 4453056243FBDA5A CRC64;
MMSFSVLQVK RLQPELITPA KSTPQETKFL SDIDDQESLR VQIPIIMCYK DNPSLNKNRN
PVKAIREALS RALVYYYPLA GRLREGPNRK LVVDCNGEGI LFVEASADVT LEQLGDKILP
PCPLLEEFLY NFPGSDGIID CPLLLIQVTC LTCGGFILAL RLNHTMCDAA GLLLFLTAIA
EMARGAHAPS ILPVWERELL FARDPPRITC AHHEYEDVIG HSDGSYASSN QSNMVQRSFY
FGAKEMRVLR KQIPPHLIST CSTFDLITAC LWKCRTLALN INPKEAVRVS CIVNARGKHN
NVRLPLGYYG NAFAFPAAIS KAEPLCKNPL GYALELVKKA KATMNEEYLR SVADLLVLRG
RPQYSSTGSY LIVSDNTRVG FGDVNFGWGQ PVFAGPVKAL DLISFYVQHK NNTEDGILVP
MCLPSSAMER FQQELERITQ EPKEDICNNL RSTSQ
