ID   ALLN1_ALLSA             Reviewed;         486 AA.
AC   Q01594;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   27-MAR-2024, entry version 128.
DE   RecName: Full=Alliin lyase 1;
DE            Short=Alliinase-1;
DE            EC=4.4.1.4 {ECO:0000269|PubMed:12136147};
DE   AltName: Full=Cysteine sulphoxide lyase 1;
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], AND PROTEIN SEQUENCE OF 39-58.
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).
RN   [2]
RP   CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, AND CRYSTALLIZATION.
RX   PubMed=12136147; DOI=10.1107/s0907444902010466;
RA   Shimon L.J., Rabinkov A., Miron T., Mirelman D., Wilchek M., Frolow F.;
RT   "Alliin lyase (alliinase) from garlic (Allium sativum): crystallization and
RT   preliminary X-ray characterization.";
RL   Acta Crystallogr. D 58:1335-1337(2002).
RN   [3]
RP   CHARACTERIZATION, AND CRYSTALLIZATION.
RC   TISSUE=Bulb;
RX   PubMed=12051663; DOI=10.1016/s0003-9861(02)00088-7;
RA   Kuettner E.B., Hilgenfeld R., Weiss M.S.;
RT   "Purification, characterization, and crystallization of alliinase from
RT   garlic.";
RL   Arch. Biochem. Biophys. 402:192-200(2002).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) OF 39-465 IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE AND CHLORIDE, COFACTOR, SUBUNIT, TISSUE SPECIFICITY,
RP   GLYCOSYLATION AT ASN-184 AND ASN-366, AND DISULFIDE BONDS.
RC   TISSUE=Bulb;
RX   PubMed=12235163; DOI=10.1074/jbc.m208669200;
RA   Kuettner E.B., Hilgenfeld R., Weiss M.S.;
RT   "The active principle of garlic at atomic resolution.";
RL   J. Biol. Chem. 277:46402-46407(2002).
RN   [5] {ECO:0007744|PDB:2HOR, ECO:0007744|PDB:2HOX}
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 39-465 OF APO- AND HOLOENZYME IN
RP   COMPLEX WITH CHLORIDE, COFACTOR, SUBUNIT, TISSUE SPECIFICITY, GLYCOSYLATION
RP   AT ASN-184; ASN-229 AND ASN-366, DISULFIDE BONDS, AND REACTION MECHANISM.
RX   PubMed=17174334; DOI=10.1016/j.jmb.2006.11.041;
RA   Shimon L.J., Rabinkov A., Shin I., Miron T., Mirelman D., Wilchek M.,
RA   Frolow F.;
RT   "Two structures of alliinase from Alliium sativum L.: apo form and ternary
RT   complex with aminoacrylate reaction intermediate covalently bound to the
RT   PLP cofactor.";
RL   J. Mol. Biol. 366:611-625(2007).
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.
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:12136147};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:12235163, ECO:0000269|PubMed:17174334};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12136147,
CC       ECO:0000269|PubMed:12235163, ECO:0000269|PubMed:17174334}.
CC   -!- SUBCELLULAR LOCATION: Vacuole.
CC   -!- TISSUE SPECIFICITY: Expressed in bulb (at protein level)
CC       (PubMed:12136147, PubMed:12235163, PubMed:17174334). Expressed in
CC       shoots. {ECO:0000269|PubMed:12136147, ECO:0000269|PubMed:12235163,
CC       ECO:0000269|PubMed:17174334}.
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   -!- 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; Z12622; CAA78268.1; -; mRNA.
DR   PIR; S29302; S29302.
DR   PDB; 1LK9; X-ray; 1.53 A; A/B=39-486.
DR   PDB; 2HOR; X-ray; 1.60 A; A=39-465.
DR   PDB; 2HOX; X-ray; 1.40 A; A/B/C/D=39-465.
DR   PDBsum; 1LK9; -.
DR   PDBsum; 2HOR; -.
DR   PDBsum; 2HOX; -.
DR   AlphaFoldDB; Q01594; -.
DR   SMR; Q01594; -.
DR   Allergome; 843; All s Alliin lyase.
DR   iPTMnet; Q01594; -.
DR   BioCyc; MetaCyc:MONOMER-13504; -.
DR   EvolutionaryTrace; Q01594; -.
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; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA: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   1: Evidence at protein level;
KW   3D-structure; Chloride; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Lyase; Pyridoxal phosphate; Schiff base;
KW   Signal; Vacuole.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..38
FT                   /evidence="ECO:0000269|PubMed:1385120"
FT                   /id="PRO_0000020677"
FT   CHAIN           39..486
FT                   /note="Alliin lyase 1"
FT                   /id="PRO_0000020678"
FT   DOMAIN          51..97
FT                   /note="EGF-like; atypical"
FT   BINDING         130..138
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000269|PubMed:12235163,
FT                   ECO:0007744|PDB:1LK9"
FT   MOD_RES         289
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:12235163,
FT                   ECO:0007744|PDB:1LK9"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:12235163, ECO:0000269|PubMed:17174334,
FT                   ECO:0007744|PDB:1LK9, ECO:0007744|PDB:2HOX"
FT   CARBOHYD        229
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:17174334, ECO:0007744|PDB:2HOX"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT                   ECO:0000269|PubMed:12235163, ECO:0000269|PubMed:17174334,
FT                   ECO:0007744|PDB:1LK9, ECO:0007744|PDB:2HOX"
FT   DISULFID        58..77
FT                   /evidence="ECO:0000269|PubMed:12235163,
FT                   ECO:0000269|PubMed:17174334, ECO:0007744|PDB:1LK9,
FT                   ECO:0007744|PDB:2HOX"
FT   DISULFID        79..88
FT                   /evidence="ECO:0000269|PubMed:12235163,
FT                   ECO:0000269|PubMed:17174334, ECO:0007744|PDB:1LK9,
FT                   ECO:0007744|PDB:2HOX"
FT   DISULFID        82..95
FT                   /evidence="ECO:0000269|PubMed:12235163,
FT                   ECO:0000269|PubMed:17174334, ECO:0007744|PDB:1LK9,
FT                   ECO:0007744|PDB:2HOX"
FT   DISULFID        406..414
FT                   /evidence="ECO:0000269|PubMed:12235163,
FT                   ECO:0000269|PubMed:17174334, ECO:0007744|PDB:1LK9,
FT                   ECO:0007744|PDB:2HOX"
FT   HELIX           44..54
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           105..107
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           108..111
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           115..118
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          120..122
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   TURN            124..127
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          129..131
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           141..154
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          163..168
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           169..181
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           204..212
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          218..223
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           224..227
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           233..235
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          236..243
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   TURN            245..247
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          259..263
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   TURN            269..271
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          281..286
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           287..290
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           294..296
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          299..303
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           306..319
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:1LK9"
FT   HELIX           325..345
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           352..371
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          374..378
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          386..388
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   TURN            389..392
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          393..395
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          400..406
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           409..411
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           414..420
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           428..431
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   STRAND          437..441
FT                   /evidence="ECO:0007829|PDB:2HOX"
FT   HELIX           446..460
FT                   /evidence="ECO:0007829|PDB:2HOX"
SQ   SEQUENCE   486 AA;  55639 MW;  D7862E867AD74383 CRC64;
     MVESYKKIGS CNKMPCLVIL TCIIMSNSLV NNNNMVQAKM TWTMKAAEEA EAVANINCSE
     HGRAFLDGII SEGSPKCECN TCYTGPDCSE KIQGCSADVA SGDGLFLEEY WKQHKEASAV
     LVSPWHRMSY FFNPVSNFIS FELEKTIKEL HEVVGNAAAK DRYIVFGVGV TQLIHGLVIS
     LSPNMTATPD APESKVVAHA PFYPVFREQT KYFNKKGYVW AGNAANYVNV SNPEQYIEMV
     TSPNNPEGLL RHAVIKGCKS IYDMVYYWPH YTPIKYKADE DILLFTMSKF TGHSGSRFGW
     ALIKDESVYN NLLNYMTKNT EGTPRETQLR SLKVLKEVVA MVKTQKGTMR DLNTFGFKKL
     RERWVNITAL LDQSDRFSYQ ELPQSEYCNY FRRMRPPSPS YAWVKCEWEE DKDCYQTFQN
     GRINTQNGVG FEASSRYVRL SLIKTQDDFD QLMYYLKDMV KAKRKTPLIK QLFIDQTETA
     SRRPFI
//