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DMDA_RUEPO
ID   DMDA_RUEPO              Reviewed;         364 AA.
AC   Q5LS57;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Dimethylsulfonioproprionate demethylase DmdA;
DE            EC=2.1.1.269 {ECO:0000269|PubMed:18849431};
GN   Name=dmdA {ECO:0000303|PubMed:21562561}; OrderedLocusNames=SPO1913;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; 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, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=17068264; DOI=10.1126/science.1130657;
RA   Howard E.C., Henriksen J.R., Buchan A., Reisch C.R., Burgmann H., Welsh R.,
RA   Ye W., Gonzalez J.M., Mace K., Joye S.B., Kiene R.P., Whitman W.B.,
RA   Moran M.A.;
RT   "Bacterial taxa that limit sulfur flux from the ocean.";
RL   Science 314:649-652(2006).
RN   [4]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=18849431; DOI=10.1128/jb.00770-08;
RA   Reisch C.R., Moran M.A., Whitman W.B.;
RT   "Dimethylsulfoniopropionate-dependent demethylase (DmdA) from Pelagibacter
RT   ubique and Silicibacter pomeroyi.";
RL   J. Bacteriol. 190:8018-8024(2008).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=21562561; DOI=10.1038/nature10078;
RA   Reisch C.R., Stoudemayer M.J., Varaljay V.A., Amster I.J., Moran M.A.,
RA   Whitman W.B.;
RT   "Novel pathway for assimilation of dimethylsulphoniopropionate widespread
RT   in marine bacteria.";
RL   Nature 473:208-211(2011).
RN   [6]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=22563425; DOI=10.1371/journal.pone.0035947;
RA   Todd J.D., Curson A.R., Sullivan M.J., Kirkwood M., Johnston A.W.;
RT   "The Ruegeria pomeroyi acuI gene has a role in DMSP catabolism and
RT   resembles yhdH of E. coli and other bacteria in conferring resistance to
RT   acrylate.";
RL   PLoS ONE 7:E35947-E35947(2012).
CC   -!- FUNCTION: Involved in the assimilation of dimethylsulphoniopropionate
CC       (DMSP), an important compound in the fixation of carbon in marine
CC       phytoplankton, by mediating demethylation of
CC       dimethylsulfonioproprionate (DMSP) to methyl-mercaptopropionate (MMPA).
CC       The intracellular concentration of DMSP is estimated to be 70 mM.
CC       {ECO:0000269|PubMed:17068264, ECO:0000269|PubMed:18849431,
CC       ECO:0000269|PubMed:21562561, ECO:0000269|PubMed:22563425}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5,6,7,8-tetrahydrofolate + S,S-dimethyl-beta-propiothetin
CC         = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3-
CC         (methylsulfanyl)propanoate + H(+); Xref=Rhea:RHEA:35467,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16457, ChEBI:CHEBI:18608,
CC         ChEBI:CHEBI:49016, ChEBI:CHEBI:57453; EC=2.1.1.269;
CC         Evidence={ECO:0000269|PubMed:18849431};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.26 mM for tetrahydrafolate {ECO:0000269|PubMed:18849431};
CC         KM=8.6 mM for dimethylsulfonioproprionate
CC         {ECO:0000269|PubMed:18849431};
CC         Vmax=0.0105 umol/min/mg enzyme {ECO:0000269|PubMed:18849431};
CC         Note=In extracts of strain DSS-3.;
CC       pH dependence:
CC         Optimum pH is 7.0-8.0. {ECO:0000269|PubMed:18849431};
CC   -!- INDUCTION: By dimethylsulfonioproprionate (DMSP) and acrylate.
CC       {ECO:0000269|PubMed:22563425}.
CC   -!- DISRUPTION PHENOTYPE: Loss of DMSP demethylation to MMPA. 25-fold
CC       increased sensitivity to acrylate, growth is strongly inhibited by 20
CC       mM dimethylsulfonioproprionate (DMSP). Disruption of this gene has a
CC       polar effect on acuI, the downstream gene, which accounts for the
CC       increased sensitivity. Dimethyl sulfide (DMS) production is enhanced.
CC       {ECO:0000269|PubMed:17068264, ECO:0000269|PubMed:21562561,
CC       ECO:0000269|PubMed:22563425}.
CC   -!- MISCELLANEOUS: DMSP is used as an intracellular osmolyte, predator
CC       deterrent and antioxidant. {ECO:0000305|PubMed:17068264}.
CC   -!- SIMILARITY: Belongs to the GcvT family. DmdA subfamily. {ECO:0000305}.
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DR   EMBL; CP000031; AAV95190.1; -; Genomic_DNA.
DR   RefSeq; WP_011047644.1; NC_003911.12.
DR   AlphaFoldDB; Q5LS57; -.
DR   SMR; Q5LS57; -.
DR   STRING; 246200.SPO1913; -.
DR   EnsemblBacteria; AAV95190; AAV95190; SPO1913.
DR   KEGG; sil:SPO1913; -.
DR   eggNOG; COG0404; Bacteria.
DR   HOGENOM; CLU_007884_10_2_5; -.
DR   OMA; MLNDPVA; -.
DR   OrthoDB; 282830at2; -.
DR   BioCyc; MetaCyc:MON-14220; -.
DR   BRENDA; 2.1.1.269; 8123.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.120; -; 1.
DR   InterPro; IPR028896; GCST/YgfZ/DmdA.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   InterPro; IPR029043; GcvT/YgfZ_C.
DR   InterPro; IPR027266; TrmE/GcvT_dom1.
DR   PANTHER; PTHR43757; PTHR43757; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
DR   SUPFAM; SSF101790; SSF101790; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..364
FT                   /note="Dimethylsulfonioproprionate demethylase DmdA"
FT                   /id="PRO_0000420617"
SQ   SEQUENCE   364 AA;  39895 MW;  070A7BD82AA5CE88 CRC64;
     MASIFPSRRV RRTPFSAGVE AAGVKGYTVY NHMLLPTVFD SLQADCAHLK EHVQVWDVAC
     ERQVSIQGPD ALRLMKLISP RDMDRMADDQ CYYVPTVDHR GGMLNDPVAV KLAADHYWLS
     LADGDLLQFG LGIAIARGFD VEIVEPDVSP LAVQGPRADD LMARVFGEAV RDIRFFRYKR
     LAFQGVELVV ARSGWSKQGG FEIYVEGSEL GMPLWNALFA AGADLNVRAG CPNNIERVES
     GLLSYGNDMT RENTPYECGL GKFCNSPEDY IGKAALAEQA KNGPARQIRA LVIGGEIPPC
     QDAWPLLADG RQVGQVGSAI HSPEFGVNVA IGMVDRSHWA PGTGMEVETP DGMRPVTVRE
     GFWR
 
 
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