ID   DDDY_ALCFA              Reviewed;         401 AA.
AC   E7DDH2;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   08-MAR-2011, sequence version 1.
DT   25-MAY-2022, entry version 23.
DE   RecName: Full=Dimethylsulfonioproprionate lyase DddY {ECO:0000305};
DE            Short=DMSP lyase;
DE            EC=4.4.1.3 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=dddY {ECO:0000312|EMBL:ADT64689.1};
OS   Alcaligenes faecalis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Alcaligenes.
OX   NCBI_TaxID=511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=M3A;
RX   PubMed=21248856; DOI=10.1038/ismej.2010.203;
RA   Curson A.R., Sullivan M.J., Todd J.D., Johnston A.W.;
RT   "DddY, a periplasmic dimethylsulfoniopropionate lyase found in
RT   taxonomically diverse species of Proteobacteria.";
RL   ISME J. 5:1191-1200(2011).
CC   -!- FUNCTION: Able to cleave dimethylsulfonioproprionate (DMSP), releasing
CC       dimethyl sulfide (DMS). DMS is the principal form by which sulfur is
CC       transported from oceans to the atmosphere.
CC       {ECO:0000269|PubMed:21248856}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S,S-dimethyl-beta-propiothetin = acrylate + dimethyl sulfide +
CC         H(+); Xref=Rhea:RHEA:19965, ChEBI:CHEBI:15378, ChEBI:CHEBI:16457,
CC         ChEBI:CHEBI:17437, ChEBI:CHEBI:37080; EC=4.4.1.3;
CC         Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC       Periplasm {ECO:0000269|PubMed:21248856}.
CC   -!- DISRUPTION PHENOTYPE: Cells are unable to produce dimethyl sulfide
CC       (DMS) from dimethylsulfonioproprionate (DMSP). Cells however grow
CC       normally on DMSP as sole carbon source. {ECO:0000269|PubMed:21248856}.
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DR   EMBL; HQ226120; ADT64689.1; -; Genomic_DNA.
DR   AlphaFoldDB; E7DDH2; -.
DR   SMR; E7DDH2; -.
DR   BRENDA; 4.4.1.3; 232.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047869; F:dimethylpropiothetin dethiomethylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR031723; DMSP_lyase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF16867; DMSP_lyase; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Lipoprotein; Lyase; Membrane; Palmitate; Periplasm; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           16..401
FT                   /note="Dimethylsulfonioproprionate lyase DddY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_0000433901"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   401 AA;  45508 MW;  4E3A44FED203F527 CRC64;
     MQKRMLGGMV AGALACFQVQ AAQFQCQDDV KPAAISAEEQ KLVDQFWAES LVYLEQYLKA
     LETPTGQCKD SAQATIQTYH SETGKAQTRC IMKYRDMELL AKHLKAVLAE PDKAKACFDP
     QKNYKEFTLY TPSSQVQQLS ATSTWINRPL LTDYYTKMGG AIGAAGLELN ENFLAITSRT
     DTTAHWTRDV SIKGLPTLWS SVGWVPLYAE NPAAGSDRFR GGYLYAELMG PWGNLRIKEI
     NGEKVGAEIG MTVQLFNTSY PFHYHHPQET YMTLTKPQCV DQNKYMVMHW DSDQFTQTRS
     DKGWTVEIDG SKERWKKWFA NQDVNKEWLT YFERNAIHAF HALEGCNQTI QNSGLVAVWA
     RSTSQDNEQF TQLCRPASGP DGVKRMRPGQ KTVCDVRDWK P