ALLN_ALLCG
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 03-AUG-2022, entry version 100.
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; Magnoliopsida; 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., 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 S-
CC 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 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}.
CC -!- SIMILARITY: Belongs to the alliinase family. {ECO:0000305}.
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DR EMBL; Z12620; CAA78266.1; -; mRNA.
DR PIR; S29300; S29300.
DR AlphaFoldDB; P31756; -.
DR SMR; P31756; -.
DR Allergome; 1254; All a Alliin lyase.
DR BioCyc; MetaCyc:MON-13494; -.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0047654; F:alliin lyase activity; ISS: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 2: Evidence at transcript level;
KW Chloride; Disulfide bond; EGF-like domain; Glycoprotein; Lyase;
KW Pyridoxal phosphate; Vacuole.
FT PROPEP <1..2
FT /id="PRO_0000020681"
FT CHAIN 3..447
FT /note="Alliin lyase"
FT /id="PRO_0000020682"
FT DOMAIN 15..61
FT /note="EGF-like; atypical"
FT BINDING 94..102
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:Q01594"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q01594"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q01594,
FT ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q01594,
FT ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250|UniProtKB:Q01594,
FT ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 22..41
FT /evidence="ECO:0000250|UniProtKB:Q01594"
FT DISULFID 43..52
FT /evidence="ECO:0000250|UniProtKB:Q01594"
FT DISULFID 46..59
FT /evidence="ECO:0000250|UniProtKB:Q01594"
FT DISULFID 370..378
FT /evidence="ECO:0000250|UniProtKB:Q01594"
FT NON_TER 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