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 02-SEP-2026, entry version 66. DE RecName: Full=Lachrymatory-factor synthase {ECO:0000303|PubMed:12384686}; DE EC=5.3.99.12 {ECO:0000269|PubMed:12384686}; DE Flags: Precursor; GN Name=LFS {ECO:0000303|PubMed:12384686}; 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], PROTEIN SEQUENCE OF 13-22, FUNCTION, AND RP CATALYTIC ACTIVITY. 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). RN [2] RP FUNCTION, AND BIOTECHNOLOGY. RX PubMed=18583530; DOI=10.1104/pp.108.123273; RA Eady C.C., Kamoi T., Kato M., Porter N.G., Davis S., Shaw M., Kamoi A., RA Imai S.; RT "Silencing onion lachrymatory factor synthase causes a significant change RT in the sulfur secondary metabolite profile."; RL Plant Physiol. 147:2096-2106(2008). RN [3] RP FUNCTION, AND MUTAGENESIS OF ARG-71 AND GLU-88. RX PubMed=22451383; DOI=10.1271/bbb.110652; RA Masamura N., Ohashi W., Tsuge N., Imai S., Ishii-Nakamura A., Hirota H., RA Nagata T., Kumagai H.; RT "Identification of amino acid residues essential for onion lachrymatory RT factor synthase activity."; RL Biosci. Biotechnol. Biochem. 76:447-453(2012). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 25-169, REACTION MECHANISM, AND RP ACTIVE SITE. RX PubMed=28708375; DOI=10.1021/acschembio.7b00336; RA Silvaroli J.A., Pleshinger M.J., Banerjee S., Kiser P.D., Golczak M.; RT "Enzyme that makes you cry-crystal structure of lachrymatory factor RT synthase from Allium cepa."; RL ACS Chem. Biol. 12:2296-2304(2017). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS). RX DOI=10.1021/acscatal.9b03720; RA Arakawa T., Sato Y., Yamada M., Takabe J., Yoshitaka Moriwaki Y., RA Masamura N., Kato M., Aoyagi M., Kamoi T., Terada T., Shimizu K., Tsuge N., RA Imai S., Fushinobu S.; RT "Dissecting the stereocontrolled conversion of short-lived sulfenic acid by RT lachrymatory factor synthase."; RL ACS Catal. 10:9-19(2020). 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. {ECO:0000269|PubMed:12384686, ECO:0000269|PubMed:18583530, CC ECO:0000269|PubMed:22451383}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-prop-1-en-1-SO-peroxol = (Z)-propanethial S-oxide; CC Xref=Rhea:RHEA:69340, ChEBI:CHEBI:183057, ChEBI:CHEBI:183657; CC EC=5.3.99.12; Evidence={ECO:0000269|PubMed:12384686}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(E)-alk-1-en-1-SO-peroxol = (Z)-alkanethial oxide; CC Xref=Rhea:RHEA:69336, ChEBI:CHEBI:183056, ChEBI:CHEBI:183059; CC EC=5.3.99.12; Evidence={ECO:0000269|PubMed:12384686}; CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305}. CC -!- BIOTECHNOLOGY: Silencing lachrymatory-factor synthase (LFS) by RNA CC interference results in a non-lachrymal onion that still retains its CC characteristic flavor and high nutritional value. CC {ECO:0000269|PubMed:18583530}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=No LFS, no cry - Issue 28 of CC November 2002; CC URL="https://www.proteinspotlight.org/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 AlphaFoldDB; P59082; -. DR SMR; P59082; -. DR KEGG; ag:BAC21275; -. DR BioCyc; MetaCyc:MONOMER-13498; -. DR BRENDA; 5.3.99.12; 248. 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; IPR053249; LFS. 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. DR PDBsum; 5GTE; -. DR PDBsum; 5GTF; -. DR PDBsum; 5GTG; -. DR PDBsum; 5VGL; -. DR PDBsum; 5VGS; -. DR PDBsum; 6IES; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Isomerase; 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 ACT_SITE 88 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000305|PubMed:28708375" FT ACT_SITE 102 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000305|PubMed:28708375" FT SITE 88 FT /note="Lowers pKa of active site Glu" FT /evidence="ECO:0000269|PubMed:28708375" FT MUTAGEN 71 FT /note="R->L: Abolishes enzyme activity; when associated FT with Q-88." FT /evidence="ECO:0000269|PubMed:22451383" FT MUTAGEN 88 FT /note="E->Q: Abolishes enzyme activity; when associated FT with L-71." FT /evidence="ECO:0000269|PubMed:22451383" 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 //