ID   DDDD_MARMS              Reviewed;         837 AA.
AC   A6W2K8;
DT   16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=CoA-transferase/lyase DddD {ECO:0000305};
DE            EC=2.-.-.- {ECO:0000269|PubMed:25140443};
GN   Name=dddD {ECO:0000312|EMBL:ABR72937.1};
GN   OrderedLocusNames=Mmwyl1_4041 {ECO:0000312|EMBL:ABR72937.1};
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17272727; DOI=10.1126/science.1135370;
RA   Todd J.D., Rogers R., Li Y.G., Wexler M., Bond P.L., Sun L., Curson A.R.,
RA   Malin G., Steinke M., Johnston A.W.;
RT   "Structural and regulatory genes required to make the gas dimethyl sulfide
RT   in bacteria.";
RL   Science 315:666-669(2007).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-602.
RX   PubMed=25140443; DOI=10.1021/bi500853s;
RA   Alcolombri U., Laurino P., Lara-Astiaso P., Vardi A., Tawfik D.S.;
RT   "DddD is a CoA-transferase/lyase producing dimethyl sulfide in the marine
RT   environment.";
RL   Biochemistry 53:5473-5475(2014).
CC   -!- FUNCTION: Dimethyl sulfide (DMS)-producing enzyme (PubMed:17272727,
CC       PubMed:25140443). Acts both as a transferase and a lyase: uses acetyl-
CC       coenzyme A (acetyl-coA) and dimethylsulfonioproprionate (DMSP) as
CC       substrates to produce DMS, acetate and 3-hydroxypropionate-CoA (3HP-
CC       CoA). Mediates the CoA-transferase prior to lyase activity
CC       (PubMed:25140443). DMS is the principal form by which sulfur is
CC       transported from oceans to the atmosphere and is a key component of the
CC       ocean sulfur cycle (PubMed:17272727, PubMed:25140443).
CC       {ECO:0000269|PubMed:17272727, ECO:0000269|PubMed:25140443}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=67 uM for acetyl-CoA {ECO:0000269|PubMed:25140443};
CC         Note=kcat is 10.8 sec(-1). {ECO:0000269|PubMed:25140443};
CC   -!- DISRUPTION PHENOTYPE: Cells are unable to grow on
CC       dimethylsulfonioproprionate (DMSP) as sole carbon source.
CC       {ECO:0000269|PubMed:17272727}.
CC   -!- MISCELLANEOUS: At least 10 million metric tons of volatile dimethyl
CC       sulfide (DMS) are released into the atmosphere annually by the
CC       dimethylsulfonioproprionate lyase in oceans. It is a component of the
CC       tangy aroma of the seaside and functions as a chemical attractant that
CC       guides various marine animals, such as sea birds, invertebrates, and
CC       some mammals, toward potential food supplies. DMS oxidation products
CC       act as condensation nuclei, causing water molecules to coalesce, with
CC       possible effects on local climate through enhanced cloud formation.
CC       {ECO:0000305|PubMed:25140443}.
CC   -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR   EMBL; CP000749; ABR72937.1; -; Genomic_DNA.
DR   RefSeq; WP_012071702.1; NC_009654.1.
DR   AlphaFoldDB; A6W2K8; -.
DR   SMR; A6W2K8; -.
DR   STRING; 400668.Mmwyl1_4041; -.
DR   PRIDE; A6W2K8; -.
DR   EnsemblBacteria; ABR72937; ABR72937; Mmwyl1_4041.
DR   KEGG; mmw:Mmwyl1_4041; -.
DR   eggNOG; COG1804; Bacteria.
DR   HOGENOM; CLU_010587_2_0_6; -.
DR   OMA; NVIAGPH; -.
DR   OrthoDB; 969868at2; -.
DR   BioCyc; MetaCyc:MON-14240; -.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1540.10; -; 2.
DR   Gene3D; 3.40.50.10540; -; 3.
DR   InterPro; IPR003673; CoA-Trfase_fam_III.
DR   InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR   InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR   Pfam; PF02515; CoA_transf_3; 2.
DR   SUPFAM; SSF89796; SSF89796; 2.
PE   1: Evidence at protein level;
KW   Lyase; Transferase.
FT   CHAIN           1..837
FT                   /note="CoA-transferase/lyase DddD"
FT                   /id="PRO_0000433895"
FT   ACT_SITE        602
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000305|PubMed:25140443"
FT   MUTAGEN         602
FT                   /note="D->A: Abolishes ability to produce dimethyl sulfide
FT                   (DMS)."
FT                   /evidence="ECO:0000269|PubMed:25140443"
SQ   SEQUENCE   837 AA;  92249 MW;  3D1AE4F4536ADD6F CRC64;
     MNKQNQLPLV GVRVADFGQQ IAGPAVAMVL ADLGATVVHI DPPGGPSWKH PANAILNRNK
     ASLCIDLKTQ AGLDQALELI ENVDIVIESF RPGVMKRLGI DFVALRESRP ELITLSMPGF
     ASNDELHRDW KATEAIVAAT SGTFTDMGFN RVLMGLNPSF SPLPLGSSYA ISLAASSIAL
     ALFEREKTGR GDNIEVPIAA ALMEGLSYNS YVVDQLPERY KTMRELEIEH RKSNNIKMDV
     SYAQLQEYLD PFYRTYVCAD GRQFYCVCPS HRNHAERALK VLGIYDELVA EGLPEVKDLH
     VPISEWDGET SIGVYPLPKK WADLISEKMK KAFLQKTSDE WGVIFGEGQI PGAPHRSTEE
     WVNSEHCNAS GLIVEVEGTE FGTMKQPGPI VWFENESEAM LKPKPQEHVS FEQALARLQS
     VAKIEKISRP TGQDIQPASG KGWLDGVKIL DLTNVIAGPH STAFMSRFGA EITKLDPVTP
     LYDPLIGILF TFQTGVGKQS ALVNIMTKEG REVFERLVRS VDIVVINAPD RQMKPLGLDQ
     DSLSAINPDV LFCRLDCFGG PRTGSKTNYI GYDDIIQANS GIMSRFGKPE TPEEHAHLGT
     LDVNCGFAAA LGMVIALYQK RKTGKVCRVR TSLSAVTNIA QIPFAFDYEG RAPFNEASGR
     EAMGNHALSH FYRTNSGWVF LDSHQGELAK LDAIKGLNGI QQSQDMGQFL RDQLVKESSA
     YWLKEFAAAD IACAEPFSIE YLREHNSRVA DQKVGTDLGS YAFSIFPDHP SGHCITQVDP
     YSIRPREAKI RAVTPTEKFG CSTIKVLQGL GYSESDINDM LEKKIAATGW GREFLPS