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 13-SEP-2023, entry version 61. 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:MONOMER-13498; -. DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell. DR CDD; cd07821; PYR_PYL_RCAR_like; 1. DR Gene3D; 3.30.530.20; -; 1. DR InterPro; IPR019587; Polyketide_cyclase/dehydratase. DR InterPro; IPR023393; START-like_dom_sf. DR PANTHER; PTHR33789; LACHRYMATORY-FACTOR SYNTHASE; 1. DR PANTHER; PTHR33789:SF11; OS05G0202300 PROTEIN; 1. DR Pfam; PF10604; Polyketide_cyc2; 1. DR SUPFAM; SSF55961; Bet v1-like; 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 //