ID   ALLN_ALLCG              Reviewed;         447 AA.
AC   P31756;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Alliin lyase;
DE            Short=Alliinase;
DE            EC=4.4.1.4;
DE   AltName: Full=Cysteine sulphoxide lyase;
DE   Flags: Precursor; Fragment;
OS   Allium cepa var. aggregatum (Shallot) (Allium ascalonicum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Allioideae; Allieae; Allium.
OX   NCBI_TaxID=28911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Shoot;
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}.
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DR   EMBL; Z12620; CAA78266.1; -; mRNA.
DR   PIR; S29300; S29300.
DR   AlphaFoldDB; P31756; -.
DR   SMR; P31756; -.
DR   Allergome; 1254; All a Alliin lyase.
DR   BioCyc; MetaCyc:MONOMER-13494; -.
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   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 2.10.25.30; EGF-like, alliinase; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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   PANTHER; PTHR43795:SF20; ALLIIN LYASE-LIKE; 1.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF04864; Alliinase_C; 1.
DR   Pfam; PF04863; EGF_alliinase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00022; EGF_1; 1.
PE   2: Evidence at transcript level;
KW   Chloride; Disulfide bond; EGF-like domain; Glycoprotein; Lyase;
KW   Pyridoxal phosphate; Vacuole.
FT   PROPEP          <1..2
FT                   /id="PRO_0000020681"
FT   CHAIN           3..447
FT                   /note="Alliin lyase"
FT                   /id="PRO_0000020682"
FT   DOMAIN          15..61
FT                   /note="EGF-like; atypical"
FT   BINDING         94..102
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   MOD_RES         253
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   CARBOHYD        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        148
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        193
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        22..41
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        43..52
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        46..59
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        370..378
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   NON_TER         1
SQ   SEQUENCE   447 AA;  51261 MW;  C4B389C81CCD45E7 CRC64;
     QAKVTWSLKA AEEAEAVANI NCSGHGRAFL DGILSDGSPK CECNTCYTGA DCSQKITGCS
     ADVASGDGLF LEEYWQQHKE NSAVLVSGWH RTSYFFNPVS NFISFELEKT IKELHEIVGN
     AAAKDRYIVF GVGVTQLIHG LVISLSPNMT ATPCAPQSKV VAHAPYYPVF REQTKYFDKK
     GYEWKGNAAD YVNTSTPEQF IEMVTSPNNP EGLLRHEVIK GCKSIYDMVY YWPHYTPIKY
     KADEDIMLFT MSKYTGHSGS RFGWALIKDE TVYNKLLNYM TKNTEGTSRE TQLRSLKILK
     EVTAMIKTQK GTMRDLNTFG FQKLRERWVN ITALLDKSDR FSYQKLPQSE YCNYFRRMRP
     PSPSYAWVKC EWEEDKDCYQ TFQNGRINTQ SGEGFEAGSR YVRLSLIKTK DDFDQLMYYL
     KIMVEAKRKT PLIKQLSNDQ ISRRPFI
//