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 24-JAN-2024, entry version 92.
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; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; 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 of
RT microbial molybdopterin-containing enzymes.";
RL Mol. Microbiol. 44:1575-1587(2002).
RN [2]
RP CATALYTIC ACTIVITY, FUNCTION, SUBSTRATE SPECIFICITY, SUBUNIT, AND 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 sulfidophilus.
RT The purified enzyme contains b-type haem and a pterin molybdenum
RT cofactor.";
RL Eur. J. Biochem. 239:391-396(1996).
CC -!- FUNCTION: Allows photoautotrophic growth on dimethyl sulfide (DMS) as
CC the sole electron donor. {ECO:0000269|PubMed:8706745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dimethyl sulfide + 2 Fe(III)-[cytochrome c2] + H2O = dimethyl
CC sulfoxide + 2 Fe(II)-[cytochrome c2] + 2 H(+); Xref=Rhea:RHEA:30227,
CC Rhea:RHEA-COMP:10429, Rhea:RHEA-COMP:10430, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17437, ChEBI:CHEBI:28262,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.8.2.4;
CC Evidence={ECO:0000269|PubMed:8706745};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000305|PubMed:8706745};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000305|PubMed:8706745};
CC -!- SUBUNIT: Heterotrimer of alpha, beta and gamma subunits.
CC {ECO:0000269|PubMed:8706745}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AF453479; AAN46632.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8GPG4; -.
DR SMR; Q8GPG4; -.
DR STRING; 35806.A6024_07035; -.
DR KEGG; ag:AAN46632; -.
DR eggNOG; COG0243; Bacteria.
DR BioCyc; MetaCyc:MONOMER-14242; -.
DR BRENDA; 1.8.2.4; 5384.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02776; MopB_CT_Nitrate-R-NarG-like; 1.
DR CDD; cd02750; MopB_Nitrate-R-NarG-like; 1.
DR Gene3D; 3.40.50.12440; -; 4.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR017840; DMSO_Rdtase_II_Mopterin_su.
DR InterPro; IPR037943; MopB_CT_Nitrate-R-NarG-like.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006311; TAT_signal.
DR NCBIfam; TIGR03479; DMSO_red_II_alp; 1.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
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
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT ECO:0000269|PubMed:12067345"
FT CHAIN 29..910
FT /note="Dimethylsulfide dehydrogenase subunit alpha"
FT /id="PRO_0000019174"
FT DOMAIN 59..123
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 66
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 70
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 109
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
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
//
