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Database: UniProt
Entry: P31756
LinkDB: P31756
Original site: P31756 
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   05-DEC-2018, entry version 91.
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; Magnoliophyta; 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.,
RA   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
CC         S-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
CC       a disulfide pattern different from the one found in the canonical
CC       EGFs. The function of this domain is unclear. It may be a binding
CC       site for other proteins or the docking site for a putative
CC       alliinase receptor (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
DR   EMBL; Z12620; CAA78266.1; -; mRNA.
DR   PIR; S29300; S29300.
DR   ProteinModelPortal; 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; IEA:UniProtKB-EC.
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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF04864; Alliinase_C; 1.
DR   Pfam; PF04863; EGF_alliinase; 1.
DR   SUPFAM; SSF53383; SSF53383; 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                                /FTId=PRO_0000020681.
FT   CHAIN         3    447       Alliin lyase.
FT                                /FTId=PRO_0000020682.
FT   DOMAIN       15     61       EGF-like; atypical.
FT   BINDING      96     96       Chloride. {ECO:0000250}.
FT   BINDING     100    100       Chloride. {ECO:0000250}.
FT   BINDING     102    102       Chloride. {ECO:0000250}.
FT   MOD_RES     253    253       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250}.
FT   CARBOHYD     21     21       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    148    148       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    193    193       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     22     41       {ECO:0000250}.
FT   DISULFID     43     52       {ECO:0000250}.
FT   DISULFID     46     59       {ECO:0000250}.
FT   DISULFID    370    378       {ECO:0000250}.
FT   NON_TER       1      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
//
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