ID   LFS_ALLCE               Reviewed;         169 AA.
AC   P59082;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Lachrymatory-factor synthase;
DE   Flags: Precursor;
GN   Name=LFS;
OS   Allium cepa (Onion).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Allioideae; Allieae; Allium.
OX   NCBI_TaxID=4679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 13-22.
RX   PubMed=12384686; DOI=10.1038/419685a;
RA   Imai S., Tsuge N., Tomotake M., Nagatome Y., Sawada H., Nagata T.,
RA   Kumagai H.;
RT   "An onion enzyme that makes the eyes water.";
RL   Nature 419:685-685(2002).
CC   -!- FUNCTION: Produces lacrymatory factor (propanthial S-oxide) from 1-
CC       propenylsulphenic acid, an unstable compound resulting from the
CC       degradation of trans-1-propenyl-L-cysteine sulphoxide (PRENCSO) by
CC       alliinase.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}.
CC   -!- BIOTECHNOLOGY: It may be possible to develop a non-lachrymal onion that
CC       still retains its characteristic flavor and high nutritional value by
CC       down-regulating the activity of this enzyme.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=No LFS, no cry - Issue 28 of
CC       November 2002;
CC       URL="https://web.expasy.org/spotlight/back_issues/028";
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; AB089203; BAC21275.1; -; mRNA.
DR   PDB; 5GTE; X-ray; 2.00 A; A/B/C/D=1-169.
DR   PDB; 5GTF; X-ray; 1.80 A; A/B/C/D=1-169.
DR   PDB; 5GTG; X-ray; 1.70 A; A/B/C/D/E/F/G/H=1-169.
DR   PDB; 5VGL; X-ray; 1.40 A; A=25-169.
DR   PDB; 5VGS; X-ray; 1.90 A; A=25-169.
DR   PDB; 6IES; X-ray; 1.80 A; A/B=1-169.
DR   PDBsum; 5GTE; -.
DR   PDBsum; 5GTF; -.
DR   PDBsum; 5GTG; -.
DR   PDBsum; 5VGL; -.
DR   PDBsum; 5VGS; -.
DR   PDBsum; 6IES; -.
DR   AlphaFoldDB; P59082; -.
DR   SMR; P59082; -.
DR   KEGG; ag:BAC21275; -.
DR   BioCyc; MetaCyc:MON-13498; -.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; IEA:UniProt.
DR   Gene3D; 3.30.530.20; -; 1.
DR   InterPro; IPR019587; Polyketide_cyclase/dehydratase.
DR   InterPro; IPR023393; START-like_dom_sf.
DR   Pfam; PF10604; Polyketide_cyc2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Vacuole.
FT   PROPEP          1..12
FT                   /evidence="ECO:0000269|PubMed:12384686"
FT                   /id="PRO_0000021591"
FT   CHAIN           13..169
FT                   /note="Lachrymatory-factor synthase"
FT                   /id="PRO_0000021592"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   HELIX           34..41
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   HELIX           44..50
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   STRAND          54..63
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   STRAND          70..77
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   TURN            78..81
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   STRAND          82..94
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   TURN            95..98
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   STRAND          99..109
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   STRAND          115..122
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   STRAND          128..141
FT                   /evidence="ECO:0007829|PDB:5VGL"
FT   HELIX           145..167
FT                   /evidence="ECO:0007829|PDB:5VGL"
SQ   SEQUENCE   169 AA;  19057 MW;  D1D2DBD00A244EF1 CRC64;
     MELNPGAPAV VADSANGARK WSGKVHALLP NTKPEQAWTL LKDFINLHKV MPSLSVCELV
     EGEANVVGCV RYVKGIMHPI EEEFWAKEKL VALDNKNMSY SYIFTECFTG YEDYTATMQI
     VEGPEHKGSR FDWSFQCKYI EGMTESAFTE ILQHWATEIG QKIEEVCSA