ALLN2_ALLSA
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 03-AUG-2022, entry version 107.
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 PRIDE; Q41233; -.
DR BioCyc; MetaCyc:MON-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; 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..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
