ID   DMDC_RUEPO              Reviewed;         588 AA.
AC   Q5LLW7;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=3-methylmercaptopropionyl-CoA dehydrogenase;
DE            EC=1.3.8.- {ECO:0000269|PubMed:21562561};
GN   Name=dmdC {ECO:0000303|PubMed:21562561};
GN   OrderedLocusNames=SPO3804 {ECO:0000312|EMBL:AAV97018.1};
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, CATALYTIC ACTIVITY, PATHWAY, 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).
CC   -!- FUNCTION: Involved in the assimilation of dimethylsulphoniopropionate
CC       (DMSP), an important compound in the fixation of carbon in marine
CC       phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl-
CC       CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).
CC       {ECO:0000269|PubMed:21562561}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(methylsulfanyl)propanoyl-CoA + H(+) + oxidized [electron-
CC         transfer flavoprotein] = 3-(methylsulfanyl)acryloyl-CoA + reduced
CC         [electron-transfer flavoprotein]; Xref=Rhea:RHEA:52612, Rhea:RHEA-
CC         COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, ChEBI:CHEBI:82815,
CC         ChEBI:CHEBI:84994; Evidence={ECO:0000269|PubMed:21562561};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:Q2LQP0};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow on
CC       methylmercaptopropionate (MMPA) as the sole source of carbon.
CC       {ECO:0000269|PubMed:21562561}.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; CP000031; AAV97018.1; -; Genomic_DNA.
DR   RefSeq; WP_011049476.1; NC_003911.12.
DR   AlphaFoldDB; Q5LLW7; -.
DR   SMR; Q5LLW7; -.
DR   STRING; 246200.SPO3804; -.
DR   EnsemblBacteria; AAV97018; AAV97018; SPO3804.
DR   KEGG; sil:SPO3804; -.
DR   eggNOG; COG1960; Bacteria.
DR   HOGENOM; CLU_018204_12_2_5; -.
DR   OMA; SIMKWCG; -.
DR   OrthoDB; 433393at2; -.
DR   BioCyc; MetaCyc:MON-16784; -.
DR   BRENDA; 1.3.99.B13; 8123.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
DR   GO; GO:0052890; F:oxidoreductase activity, acting on the CH-CH group of donors, with a flavin as acceptor; IDA:UniProtKB.
DR   Gene3D; 1.10.540.10; -; 1.
DR   Gene3D; 2.40.110.10; -; 1.
DR   InterPro; IPR025878; Acyl-CoA_dh-like_C_dom.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF12806; Acyl-CoA_dh_C; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF47203; SSF47203; 1.
DR   SUPFAM; SSF56645; SSF56645; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..588
FT                   /note="3-methylmercaptopropionyl-CoA dehydrogenase"
FT                   /id="PRO_0000433904"
FT   ACT_SITE        435
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q06319"
SQ   SEQUENCE   588 AA;  62854 MW;  3F4EC355B877125A CRC64;
     MTYQAPVRDI MFAIEHLSQW PQVEALQTYS EIELDDARAA LEEFGRFCGE MIAPLSTIGD
     TEGARLENGR VVLPEGYKTA YDQFVDMGWQ SLSHPAEHGG MGLPKVVGAA ATEIVNSADM
     SFGLCPLLTN GAIDALSITG SDAQKAFYLD KLITGRWSGT MNLTEPQAGS DLSRVRCTAV
     PQDDGTYAIS GTKIFITFGE HDLSENIVHL VLARTPDAPE GVRGLSLFVV PKLLAGEGGE
     TSQRNTLGCV SLEHKLGVRA SPTAVMEYDN ATGYLVGEEN SGLRYMFIMM TSARYAVGVQ
     GVAIAERAYQ HALSYARDRI QSRPVDGSAQ DAVPIIQHPD VRRMLLRMRA LTEGGRALAI
     ATGGWLDLAE HGPEEARAEA QSMAEFLVPL VKGFCTERAV EVASLGVQIH GGMGFIEETG
     VAQFYRDARI LPIYEGTTAI QANDLLGRKV LRDGGRTARR FAEMIAATEG ELSKGGAAAQ
     RIAQRLAEAR AAFAAGLDHL LATAGQDPNR AYAGSVPFLM LTGNLATGWQ LGLSALAAEA
     ELAKGGDAEF LQAKIATADI FAQQVLVECS AEHSRITDTG DSLLTASL