ALLN1_ALLSA
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 03-AUG-2022, entry version 123.
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 BioCyc; MetaCyc:MON-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 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 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
