(data stored in ACNUC9435 zone)

SWISSPROT: DDDW_RUEPO

ID   DDDW_RUEPO              Reviewed;         152 AA.
AC   Q5LW89;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   RecName: Full=Dimethlysulfonioproprionate lyase DddW {ECO:0000305};
DE            Short=DMSP lyase;
DE            EC=4.4.1.3 {ECO:0000269|PubMed:25993446};
GN   Name=dddW {ECO:0000312|EMBL:AAV93771.1};
GN   OrderedLocusNames=SPO0453 {ECO:0000312|EMBL:AAV93771.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=21677693; DOI=10.1038/ismej.2011.79;
RA   Todd J.D., Kirkwood M., Newton-Payne S., Johnston A.W.;
RT   "DddW, a third DMSP lyase in a model Roseobacter marine bacterium, Ruegeria
RT   pomeroyi DSS-3.";
RL   ISME J. 6:223-226(2012).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   COFACTOR, AND MUTAGENESIS OF HIS-81; HIS-83; GLU-87 AND HIS-121.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25993446; DOI=10.1371/journal.pone.0127288;
RA   Brummett A.E., Schnicker N.J., Crider A., Todd J.D., Dey M.;
RT   "Biochemical, kinetic, and spectroscopic characterization of Ruegeria
RT   pomeroyi DddW-A mononuclear iron-dependent DMSP lyase.";
RL   PLoS ONE 10:E0127288-E0127288(2015).
CC   -!- FUNCTION: Able to cleave dimethlysulfonioproprionate (DMSP), releasing
CC       dimethyl sulfide (DMS) and acrylate. DMS is the principal form by which
CC       sulfur is transported from oceans to the atmosphere.
CC       {ECO:0000269|PubMed:21677693, ECO:0000269|PubMed:25993446}.
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:0000269|PubMed:25993446};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:25993446};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:25993446};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.68 uM for dimethlysulfonioproprionate (in the presence of
CC         Fe(2+)) {ECO:0000269|PubMed:25993446};
CC         KM=4.50 uM for dimethlysulfonioproprionate (in the presence of
CC         Mn(2+)) {ECO:0000269|PubMed:25993446};
CC         Note=Kcat is 18,25 sec(-1) with dimethlysulfonioproprionate (in the
CC         presence of Fe(2+)). Kcat is 17.33 sec(-1) with
CC         dimethlysulfonioproprionate (in the presence of Mn(2+).
CC         {ECO:0000269|PubMed:25993446};
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|PubMed:25993446};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25993446}.
CC   -!- INDUCTION: Up-regulated by pre-growth of cells with
CC       dimethlysulfonioproprionate (DMSP). {ECO:0000269|PubMed:21677693}.
CC   -!- DISRUPTION PHENOTYPE: Decreased production of dimethyl sulfide (DMS).
CC       {ECO:0000269|PubMed:21677693}.
CC   -!- SIMILARITY: Belongs to the non-heme iron-dependent dioxygenase family.
CC       {ECO:0000305}.
DR   EMBL; CP000031; AAV93771.1; -; Genomic_DNA.
DR   RefSeq; WP_011046214.1; NC_003911.12.
DR   SMR; Q5LW89; -.
DR   STRING; 246200.SPO0453; -.
DR   EnsemblBacteria; AAV93771; AAV93771; SPO0453.
DR   KEGG; sil:SPO0453; -.
DR   eggNOG; ENOG4106BM2; Bacteria.
DR   eggNOG; ENOG4111WK5; LUCA.
DR   HOGENOM; HOG000234873; -.
DR   OMA; GHLCAHR; -.
DR   OrthoDB; 1928636at2; -.
DR   BioCyc; RPOM246200:G1G48-460-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0047869; F:dimethylpropiothetin dethiomethylase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR013096; Cupin_2.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF07883; Cupin_2; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q5LW89.
DR   SWISS-2DPAGE; Q5LW89.
KW   Lyase; Metal-binding; Reference proteome.
FT   CHAIN           1..152
FT                   /note="Dimethlysulfonioproprionate lyase DddW"
FT                   /id="PRO_0000433900"
FT   METAL           83
FT                   /note="Iron; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:25993446"
FT   METAL           87
FT                   /note="Iron"
FT                   /evidence="ECO:0000269|PubMed:25993446"
FT   METAL           89
FT                   /note="Iron"
FT                   /evidence="ECO:0000250|UniProtKB:D0CY60"
FT   METAL           121
FT                   /note="Iron; via tele nitrogen"
FT                   /evidence="ECO:0000269|PubMed:25993446"
FT   MUTAGEN         81
FT                   /note="H->A: Decreased iron binding and enzyme activity
FT                   toward DMSP."
FT                   /evidence="ECO:0000269|PubMed:25993446"
FT   MUTAGEN         83
FT                   /note="H->A: Decreased iron binding and enzyme activity
FT                   toward DMSP."
FT                   /evidence="ECO:0000269|PubMed:25993446"
FT   MUTAGEN         87
FT                   /note="E->A: Decreased iron binding and enzyme activity
FT                   toward DMSP."
FT                   /evidence="ECO:0000269|PubMed:25993446"
FT   MUTAGEN         121
FT                   /note="H->A: Decreased iron binding and enzyme activity
FT                   toward DMSP."
FT                   /evidence="ECO:0000269|PubMed:25993446"
SQ   SEQUENCE   152 AA;  16132 MW;  90EF8584AEFCA325 CRC64;
     MTAMLDSFAT DLTAATSLHQ PGNLPHPPHA IDAENVPLSG GTDPTYGEVR WRTLINGTEA
     APRDMVLGIA EFGPGHQLRP HRHTPPEFYL GLEGSGIVTI DGVPHEIRAG VALYIPGDAE
     HGTVAGPEGL RFAYGFASAS FEAIEYRFTA SA
//

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