ID   DDHA_RHOSU              Reviewed;         910 AA.
AC   Q8GPG4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   01-MAY-2013, entry version 59.
DE   RecName: Full=Dimethylsulfide dehydrogenase subunit alpha;
DE            EC=1.8.2.4;
DE   AltName: Full=DMS DH molybdenum subunit;
DE   AltName: Full=DMS DH subunit alpha;
DE   AltName: Full=Dimethyl sulfide:cytochrome c2 reductase subunit alpha;
DE   AltName: Full=Dimethylsulfide dehydrogenase molybdenum subunit;
DE   Flags: Precursor;
GN   Name=ddhA;
OS   Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodovulum.
OX   NCBI_TaxID=35806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-38.
RC   STRAIN=SH1;
RX   PubMed=12067345; DOI=10.1046/j.1365-2958.2002.02978.x;
RA   McDevitt C.A., Hugenholtz P., Hanson G.R., McEwan A.G.;
RT   "Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum
RT   sulfidophilum: its place in the dimethyl sulphoxide reductase family
RT   of microbial molybdopterin-containing enzymes.";
RL   Mol. Microbiol. 44:1575-1587(2002).
RN   [2]
RP   CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBUNIT, AND
RP   COFACTOR.
RX   PubMed=8706745; DOI=10.1111/j.1432-1033.1996.0391u.x;
RA   Hanlon S.P., Toh T.H., Solomon P.S., Holt R.A., McEwan A.G.;
RT   "Dimethylsulfide:acceptor oxidoreductase from Rhodobacter
RT   sulfidophilus. The purified enzyme contains b-type haem and a pterin
RT   molybdenum cofactor.";
RL   Eur. J. Biochem. 239:391-396(1996).
CC   -!- FUNCTION: Allows photoautotrophic growth on dimethyl sulfide (DMS)
CC       as the sole electron donor.
CC   -!- CATALYTIC ACTIVITY: Dimethyl sulfide + 2 ferricytochrome c2 +
CC       H(2)O = dimethyl sulfoxide + 2 ferrocytochrome c2 + 2 H(+).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential).
CC   -!- COFACTOR: Molybdenum (molybdopterin).
CC   -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has been experimentally proven.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family.
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DR   EMBL; AF453479; AAN46632.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q8GPG4; -.
DR   BioCyc; MetaCyc:MONOMER-14242; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0016661; F:oxidoreductase activity, acting on other nitrogenous compounds as donors; IEA:InterPro.
DR   Gene3D; 2.40.40.20; -; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom.
DR   InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR   TIGRFAMs; TIGR03479; DMSO_red_II_alp; 1.
DR   PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; FALSE_NEG.
DR   PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW   Molybdenum; Oxidoreductase; Periplasm; Signal.
FT   SIGNAL        1     28       Tat-type signal.
FT   CHAIN        29    910       Dimethylsulfide dehydrogenase subunit
FT                                alpha.
FT                                /FTId=PRO_0000019174.
FT   METAL        66     66       Iron-sulfur (4Fe-4S); via pros nitrogen
FT                                (By similarity).
FT   METAL        70     70       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL        74     74       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       109    109       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   910 AA;  102309 MW;  8332BC7C8D8F25FB CRC64;
     MLRTTRRTLM QGASLVGAGL FAAGRGWALN RLEPIGDTLA EEYPYRDWED LYRNEFTWDY
     VGKAAHCINC LGNCAFDIYV KDGIVIREEQ LAKYPQISPD IPDANPRGCQ KGAIHSTSMY
     EADRLRYPMK RVGARGEGKW QRISWDQATE EIADKIIDIY EKYGPGKLMT HTGSGNMSMM
     RMAAPYRFAS LVGGVQLDIF TDVGDLNTGA HLAYGNALES FTSDAWFGAD YIMFLLFNPV
     ATRIPDAHFL WEAKWNGARV VSVAPDYNPS SIHSDLWMPI KQGADPFLAM SMVNVIIEGK
     LYNEAFMKEQ TDLPILVRSD NGMLLREADL EEGGSDQVFY HWDSRTGAAV KVKGSMGSEE
     KTLVLGDVDP ALEGSFEVGG IPVTTVFEKV RAEAAKYPPE ETAAITGIGP GVVRAEAETF
     ARAKKALLMT GFNIGRYSNG IYTSWALTLM LALTGHGGRT GGLDTSWIAW NQPALLELAF
     FDFKKLPRLE AGGLGEFVRG GMMEHSRQHY DNDKLKARTG FDLDELQEMI DESIDAGWMP
     YYGDMKGLIS IADNKFRRNK NAEAYRERIL EEVEELFVDI NVRMDSTAQW ADYLLPAAAH
     YEAWDLRSIA FHRFVNVFSR PVPPIGEAKS DWEIMEILTR KIQERAIARG ITGYEDGDVT
     RDFATIHDDY TMDGTLMTDH DVVSWLVENG PEFAGATLEE GVERGFFVMG EDAGPTQKLR
     PSEPYHAFLQ QTEGKEPYKT MTGRITFFVD HPRFVRLGAT VPTARHHAGR DASNYPLNFF
     SPHTRWGIHS NWRSNKFMLR LQRGEPNIYI SPQLAAAKGI ADGAQVRVFN ELSFFFAQAK
     FYPSLPPDTI MMEHGWEPHQ FPNWRPMNVC MATLLQPLEL VGGWGHLNFS LWHWNANQLA
     HESSVDIEPA
//