ID   ALLN_ALLCE              Reviewed;         479 AA.
AC   P31757;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Alliin lyase;
DE            Short=Alliinase;
DE            EC=4.4.1.4;
DE   AltName: Full=Cysteine sulphoxide lyase;
DE   Flags: Precursor;
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 35-54.
RX   PubMed=1385120; DOI=10.1111/j.1432-1033.1992.tb17344.x;
RA   van Damme E.J.M., Smeets K., Torrekens S., van Leuven F., Peumans W.J.;
RT   "Isolation and characterization of alliinase cDNA clones from garlic
RT   (Allium sativum L.) and related species.";
RL   Eur. J. Biochem. 209:751-757(1992).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an S-alkyl-L-cysteine S-oxide = 2-aminoprop-2-enoate + an S-
CC         alkyl sulfenate; Xref=Rhea:RHEA:20141, ChEBI:CHEBI:22326,
CC         ChEBI:CHEBI:76565, ChEBI:CHEBI:142409; EC=4.4.1.4;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole.
CC   -!- DOMAIN: The 6 Cys residues of the EGF-like domain are arranged in a
CC       disulfide pattern different from the one found in the canonical EGFs.
CC       The function of this domain is unclear. It may be a binding site for
CC       other proteins or the docking site for a putative alliinase receptor
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA78267.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z12621; CAA78267.1; ALT_INIT; mRNA.
DR   PIR; S29301; S29301.
DR   AlphaFoldDB; P31757; -.
DR   SMR; P31757; -.
DR   Allergome; 842; All c Alliin lyase.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0047654; F:alliin lyase activity; ISS:UniProtKB.
DR   GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   Gene3D; 2.10.25.30; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR006948; Alliinase_C.
DR   InterPro; IPR037029; Alliinase_N_sf.
DR   InterPro; IPR006947; EGF_alliinase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF04864; Alliinase_C; 1.
DR   Pfam; PF04863; EGF_alliinase; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00022; EGF_1; 1.
PE   1: Evidence at protein level;
KW   Chloride; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Lyase; Pyridoxal phosphate; Signal; Vacuole.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..34
FT                   /evidence="ECO:0000269|PubMed:1385120"
FT                   /id="PRO_0000020683"
FT   CHAIN           35..479
FT                   /note="Alliin lyase"
FT                   /id="PRO_0000020684"
FT   DOMAIN          47..93
FT                   /note="EGF-like; atypical"
FT   BINDING         126..134
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   MOD_RES         285
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        225
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        362
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        54..73
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        75..84
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        78..91
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        402..410
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   CONFLICT        37
FT                   /note="S -> T (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   479 AA;  54839 MW;  2641AB82B8990230 CRC64;
     MESYDKVGSN KVPCLLILTC IIMSSFVNNN IVQAKVSWSL KAAEEAEAVA NINCSGHGRA
     FLDGILSDGS PKCECNTCYT GADCSEKITG CSADVASGDG LFLEEYWQQH KENSAVLVSG
     WHRMSYFFNP VSNFISFELE KTIKELHEIV GNAAAKDRYI VFGVGVTQLI HGLVISLSPN
     MTATPCAPQS KVVAHAPYYP VFREQTKYFD KKGYEWKGNA ADYVNTSTPE QFIEMVTSPN
     NPEGLLRHEV IKGCKSIYYM VYYWPHYTPI KYKADEDIML FTMSKYTGHS GSRFGWALIK
     DETVYNKLLN YMTKNTEGTS RETQLRSLKI LKEVIAMVKT QNGTMRDLNT FGFQKLRERW
     VNITALLDKS DRFSYQKLPQ SEYCNYFRRM RPPSPSYAWV KCEWEEDKDC YQTFQNGRIN
     TQSGEGFEAG SRYVRLSLIK TKDDFDQLMY YLKIMVEAKR KTPLIKQLSN DQISRRPFI