ID   DDDL_CERS4              Reviewed;         232 AA.
AC   Q3J6L0;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Putative dimethylsulfonioproprionate lyase DddL;
DE            Short=DMSP lyase;
DE            EC=4.4.1.3 {ECO:0000303|PubMed:21249136};
DE   AltName: Full=Dimethylpropiothetin dethiomethylase;
GN   Name=dddL; OrderedLocusNames=RHOS4_00060; ORFNames=RSP_1433;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   POSSIBLE FUNCTION, AND INDUCTION.
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RX   PubMed=21249136; DOI=10.1371/journal.pone.0015972;
RA   Sullivan M.J., Curson A.R., Shearer N., Todd J.D., Green R.T.,
RA   Johnston A.W.;
RT   "Unusual regulation of a leaderless operon involved in the catabolism of
RT   dimethylsulfoniopropionate in Rhodobacter sphaeroides.";
RL   PLoS ONE 6:E15972-E15972(2011).
CC   -!- FUNCTION: May cleave dimethylsulfonioproprionate (DMSP), releasing
CC       dimethyl sulfide (DMS). DMS is the principal form by which sulfur is
CC       transported from oceans to the atmosphere (PubMed:21249136). The real
CC       activity of the protein is however subject to debate and it is unclear
CC       whether it constitutes a real dimethylsulfonioproprionate lyase in vivo
CC       (Probable). {ECO:0000303|PubMed:21249136, ECO:0000305}.
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:0000303|PubMed:21249136};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:D0CY60};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:D0CY60}.
CC   -!- INDUCTION: Weakly induced by acrylate and dimethylsulfonioproprionate
CC       (DMSP). Part of the acuR-acuI-dddL operon.
CC       {ECO:0000269|PubMed:21249136}.
CC   -!- MISCELLANEOUS: DMSP is used as an intracellular osmolyte, predator
CC       deterrent and antioxidant. {ECO:0000305|PubMed:21249136}.
CC   -!- SIMILARITY: Belongs to the non-heme iron-dependent dioxygenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000143; ABA77574.1; -; Genomic_DNA.
DR   RefSeq; WP_011336734.1; NZ_CP030271.1.
DR   RefSeq; YP_351475.1; NC_007493.2.
DR   AlphaFoldDB; Q3J6L0; -.
DR   SMR; Q3J6L0; -.
DR   STRING; 272943.RSP_1433; -.
DR   EnsemblBacteria; ABA77574; ABA77574; RSP_1433.
DR   GeneID; 57468776; -.
DR   KEGG; rsp:RSP_1433; -.
DR   PATRIC; fig|272943.9.peg.297; -.
DR   eggNOG; COG0662; Bacteria.
DR   OMA; FGTRGHF; -.
DR   Proteomes; UP000002703; Chromosome 1.
DR   GO; GO:0047869; F:dimethylpropiothetin dethiomethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR031723; DMSP_lyase.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF16867; DMSP_lyase; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Metal-binding; Reference proteome.
FT   CHAIN           1..232
FT                   /note="Putative dimethylsulfonioproprionate lyase DddL"
FT                   /id="PRO_0000420618"
FT   BINDING         154
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:D0CY60"
FT   BINDING         159
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:D0CY60"
FT   BINDING         161
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:D0CY60"
FT   BINDING         190
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:D0CY60"
SQ   SEQUENCE   232 AA;  25801 MW;  1CDABDA4CB36F608 CRC64;
     MHSLSERVEQ LRLNDCPDWL YLLHEFDALY RQGSDGGSRP IRTHRKRVRD SLALIVEANP
     AVNDRPPEVK PVTAHLGRAL DLGERGAVQG MSRALARVAG RLTWEYGYEK VPKALARKYA
     YCEILGPRGP ICAERLILGF VLFAPSTTYP QHSHKDIEES YISVAGAWSE NDAAVHAPGS
     LILNRPGLEH RITTGDLSPC LLAYAWTGSE ERLNQPGMKL SSPRKARIEK GI