ASAT3_SOLLC
ID ASAT3_SOLLC Reviewed; 430 AA.
AC K4D9Y4;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Acylsugar acyltransferase 3 {ECO:0000303|PubMed:25862303};
DE Short=Sl-ASAT3 {ECO:0000303|PubMed:25862303};
DE EC=2.3.1.- {ECO:0000305};
GN Name=ASAT3 {ECO:0000303|PubMed:25862303};
GN OrderedLocusNames=Solyc11g067270.1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000312|Proteomes:UP000004994};
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. M82;
RX PubMed=25862303; DOI=10.1105/tpc.15.00087;
RA Schilmiller A.L., Moghe G.D., Fan P., Ghosh B., Ning J., Jones A.D.,
RA Last R.L.;
RT "Functionally divergent alleles and duplicated Loci encoding an
RT acyltransferase contribute to acylsugar metabolite diversity in solanum
RT trichomes.";
RL Plant Cell 27:1002-1017(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Catalyzes the transfer of short (four to five carbons)
CC branched acyl chains to the furanose ring of di-acylsucrose acceptors
CC to produce tri-acylsucroses such as S3:15 (5,5,5), S4:17 (2,5,5,5) and
CC S4:24 (2,5,5,12) acylsucroses. {ECO:0000269|PubMed:25862303}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q70PR7}.
CC -!- TISSUE SPECIFICITY: Expressed in tip cells of type I trichomes of stems
CC and petioles, sites of acylsugars production.
CC {ECO:0000269|PubMed:25862303}.
CC -!- DISRUPTION PHENOTYPE: Reduced total acylsugar levels, with abnormal
CC accumulation of di-acylsucrose, S2:17 (5,12), and two triacylsucroses,
CC S3:19 (2,5,12) and S3:22 (5,5,12) lacking furanose ring acylation, but
CC impaired accumulation of S3:15 (5,5,5), S4:17 (2,5,5,5) and S4:24
CC (2,5,5,12) acylsucroses. {ECO:0000269|PubMed:25862303}.
CC -!- SIMILARITY: Belongs to the plant acyltransferase family. {ECO:0000305}.
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DR EMBL; KM516150; AJF98582.1; -; Genomic_DNA.
DR EMBL; CM001074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K4D9Y4; -.
DR SMR; K4D9Y4; -.
DR STRING; 4081.Solyc11g067270.1.1; -.
DR PaxDb; K4D9Y4; -.
DR PRIDE; K4D9Y4; -.
DR EnsemblPlants; Solyc11g067270.1.1; Solyc11g067270.1.1.1; Solyc11g067270.1.
DR Gramene; Solyc11g067270.1.1; Solyc11g067270.1.1.1; Solyc11g067270.1.
DR eggNOG; ENOG502QYCI; Eukaryota.
DR HOGENOM; CLU_014546_0_0_1; -.
DR InParanoid; K4D9Y4; -.
DR OMA; MVESTIL; -.
DR OrthoDB; 1130893at2759; -.
DR PhylomeDB; K4D9Y4; -.
DR BioCyc; MetaCyc:MON18C3-34; -.
DR Proteomes; UP000004994; Chromosome 11.
DR GO; GO:0016746; F:acyltransferase activity; IMP:UniProtKB.
DR GO; GO:0005985; P:sucrose metabolic process; IMP:UniProtKB.
DR Gene3D; 3.30.559.10; -; 2.
DR InterPro; IPR023213; CAT-like_dom_sf.
PE 2: Evidence at transcript level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..430
FT /note="Acylsugar acyltransferase 3"
FT /id="PRO_0000433637"
FT ACT_SITE 155
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
SQ SEQUENCE 430 AA; 48370 MW; DDC653A11E70C7F9 CRC64;
MASSTIISRK MIKLLSPTPS SLRCHKLSFM DHINFPLHSP YAFFYPKIPQ NYSNKISQVL
ENSLSKVLSF YYPLAGKINN NYTYVDCNDT GAEYLNVRID CPMSQILNHP YNDVVDVVFP
QDLPWSSSSL TRSPLVVQLS HFDCGGVAVS ACTSHTIFDG YCLSKFINDW ASTARNMEFK
PSPQFNASTF FPLPSETNLS STLPATRPSQ RHVSRMYNFS SSNLTRLKDI VTKESHVKNP
TRVEVASALV HKCGVTMSME SSGMFKPTLM SHAMNLRPPI PLNTMGNATC IILTTAMTED
EVKLPNFVAK LQKDKQQLRD KLKDMKEDRM PLYTLELGKN AMNIIEKDTH DVYLCSGMTN
TGLHKIDFGW GEPVRVTLAT HPNKNNFIFM DEQSGDGLNV LITLTKDDML KFQSNKELLE
FASPVVESTK