ID   ALLN2_ALLSA             Reviewed;         473 AA.
AC   Q41233;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=Alliin lyase 2 {ECO:0000303|PubMed:7979352};
DE            Short=Alliinase-2 {ECO:0000303|PubMed:7979352};
DE            EC=4.4.1.4 {ECO:0000269|PubMed:7979352};
DE   AltName: Full=Cysteine sulphoxide lyase 2 {ECO:0000303|PubMed:7979352};
DE   Flags: Precursor;
OS   Allium sativum (Garlic).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC   Allioideae; Allieae; Allium.
OX   NCBI_TaxID=4682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PARTIAL PROTEIN
RP   SEQUENCE, CHARACTERIZATION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBUNIT, AND GLYCOSYLATION.
RC   TISSUE=Bulb;
RX   PubMed=7979352; DOI=10.1007/bf02788739;
RA   Rabinkov A., Zhu X.-Z., Grafi G., Galili G., Mirelman D.;
RT   "Alliin lyase (Alliinase) from garlic (Allium sativum). Biochemical
RT   characterization and cDNA cloning.";
RL   Appl. Biochem. Biotechnol. 48:149-171(1994).
RN   [2]
RP   XXX, AND REVIEW.
RX   PubMed=25153873; DOI=10.3390/molecules190812591;
RA   Borlinghaus J., Albrecht F., Gruhlke M.C.H., Nwachukwu I.D.,
RA   Slusarenko A.J.;
RT   "Allicin: chemistry and biological properties.";
RL   Molecules 19:12591-12618(2014).
RN   [3]
RP   XXX, AND REVIEW.
RX   PubMed=32207097; DOI=10.1007/s12223-020-00786-5;
RA   Choo S., Chin V.K., Wong E.H., Madhavan P., Tay S.T., Yong P.V.C.,
RA   Chong P.P.;
RT   "Review: antimicrobial properties of allicin used alone or in combination
RT   with other medications.";
RL   Folia Microbiol. (Praha) 65:451-465(2020).
CC   -!- FUNCTION: Able to cleave the C-S bond of sulfoxide derivatives of Cys
CC       to produce allicin, thus giving rise to all sulfur compounds which are
CC       responsible for most of the properties of garlic, such as the specific
CC       smell and flavor as well as the health benefits like blood lipid or
CC       blood pressure lowering. {ECO:0000269|PubMed:7979352}.
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         Evidence={ECO:0000269|PubMed:7979352};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alliin = 2-aminoprop-2-enoate + allylsulfenate;
CC         Xref=Rhea:RHEA:54688, ChEBI:CHEBI:76565, ChEBI:CHEBI:132987,
CC         ChEBI:CHEBI:138314; EC=4.4.1.4;
CC         Evidence={ECO:0000269|PubMed:7979352};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q01594};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.1 mM for S-allylcysteine sulfoxide {ECO:0000269|PubMed:7979352};
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:7979352};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7979352}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000305|PubMed:7979352}.
CC   -!- TISSUE SPECIFICITY: High expression in bulbs, lower expression in
CC       leaves, and no expression in roots. {ECO:0000269|PubMed:7979352}.
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|UniProtKB:Q01594}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:7979352}.
CC   -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=What's that smell? - Issue
CC       39 of October 2003;
CC       URL="https://web.expasy.org/spotlight/back_issues/039";
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DR   EMBL; S73324; AAB32477.1; -; mRNA.
DR   AlphaFoldDB; Q41233; -.
DR   SMR; Q41233; -.
DR   Allergome; 843; All s Alliin lyase.
DR   BioCyc; MetaCyc:MONOMER-13491; -.
DR   BRENDA; 4.4.1.4; 252.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0047654; F:alliin lyase activity; IDA:UniProtKB.
DR   GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
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   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..15
FT                   /evidence="ECO:0000255"
FT   PROPEP          16..25
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT                   /id="PRO_0000020679"
FT   CHAIN           26..473
FT                   /note="Alliin lyase 2"
FT                   /id="PRO_0000020680"
FT   DOMAIN          38..84
FT                   /note="EGF-like; atypical"
FT   BINDING         117..125
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   MOD_RES         276
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        216
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01594,
FT                   ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        45..64
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        66..75
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        69..82
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
FT   DISULFID        393..401
FT                   /evidence="ECO:0000250|UniProtKB:Q01594"
SQ   SEQUENCE   473 AA;  54183 MW;  19F08669BA95A047 CRC64;
     MICLVILTCI IMSNSFVNNN NMVQAKMTWT MKAAEEAEAV ANINCSEHGR AFLDGIISEG
     SPKCECNTCY TGPDCSEKIQ GCSADVASGD GLFLEEYWKQ HKEASAVLVS PWHRMSYFFN
     PVSNFISFEL EKTIKELHEV VGNAAAKDRY IVFGVGVTQL IHGLVISLSP NMTATPDAPE
     SKVVAHAPFY PVFREQTKYF DKKGYVWAGN AANYVNVSNP EQYIEMVTSP NNPEGLLRHA
     VIKGCKSIYD MVYYWPHYTP IKYKADEDIL LFTMSKFTGH SGSRFGWALI KDESVYNNLL
     NYMTKNTEGT PRETQLRSLK VLKEIVAMVK TQKGTMRDLN TFGFKKLRER WVNITALLDQ
     SDRFSYQELP QSEYCNYFRR MRPPSPSYAW VNCEWEEDKD CYQTFQNGRI NTQSGVGFEA
     SSRYVRLSLI KTQDDFDQLM YYLKDMVKAK RKTPLIKQLF TDETETASRR PFI
//