ID   Q24RT7_DESHY            Unreviewed;       857 AA.
AC   Q24RT7;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Putative anaerobic DMSO reductase chain A {ECO:0000313|EMBL:BAE85255.1};
DE            EC=1.7.99.4 {ECO:0000313|EMBL:BAE85255.1};
GN   Name=dmsA {ECO:0000313|EMBL:BAE85255.1};
GN   OrderedLocusNames=DSY3466 {ECO:0000313|EMBL:BAE85255.1};
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE85255.1, ECO:0000313|Proteomes:UP000001946};
RN   [1] {ECO:0000313|EMBL:BAE85255.1, ECO:0000313|Proteomes:UP000001946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51 {ECO:0000313|EMBL:BAE85255.1,
RC   ECO:0000313|Proteomes:UP000001946};
RX   PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
CC   -!- COFACTOR:
CC       Name=Mo-bis(molybdopterin guanine dinucleotide);
CC         Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008230; BAE85255.1; -; Genomic_DNA.
DR   RefSeq; WP_011461139.1; NC_007907.1.
DR   AlphaFoldDB; Q24RT7; -.
DR   STRING; 138119.DSY3466; -.
DR   KEGG; dsy:DSY3466; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_9; -.
DR   Proteomes; UP000001946; Chromosome.
DR   GO; GO:0051536; F:iron-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:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.12440; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 2.20.25.90; ADC-like domains; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR43742:SF3; DIMETHYL SULFOXIDE REDUCTASE DMSA; 1.
DR   PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR   Pfam; PF04879; Molybdop_Fe4S4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SMART; SM00926; Molybdop_Fe4S4; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:BAE85255.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001946};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          50..111
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   857 AA;  94254 MW;  273553FCF287058A CRC64;
     MDLIDRITNA KLSRRSFILA SAAATAGLSL TGCGSSLTQA TADQAAGKEG KWITAACWHN
     CGGRCLNKAY VVDGVVIRQK TDDTHPDSPD YPQQRACVRG RSQRQQVFGA DRLKYPMKRK
     NWEPGGGKKE LRGRDEWVRI SWDEALDSIA GEIKRIKSEQ GNRAFFADGG PAAKVLALYG
     GYVANWGTTS LGSWTYTPGP VGFSSSSGDS INDRLDMRNC DTVIMFNMNP AWSSAGNPVY
     HFLQVKKAGA DFIAIDPFYN DSYGLLEADW IPTRPATDTA LMIGVAHTLI VEDDPVKNPL
     IDWDFLKKYT IGFDADSMPP GTDAKDNFKD YVLGTYDGVP KNAEWAAEIS GVAPDRIRYL
     ARAMNKNKKV ALLYAWSAGR TQNADNLPQM AMILGAMTGH MGKSGHMCGV SCHSGAANGG
     DTLVSPGKNG LPTVDNPVKD SINHTEMWRA IVDGKYNFTG NKKFLKGEMR DIDIRLIYHD
     NNARLQSADG MTKGIEAHRK VDLVVSHGQF LTTNAKYSDF VLPVTTEWEK IGGFLTGNRE
     MLIMYSQITE PLYEAQSDEW IARELAKRLG VDASKAFPID AKQQFFNQIA GSTVILPDGK
     TAAPLVTITA EDIAQWGVQG KPQQGQISLK EFQEKGLYQI ERKPGDNYGY IAFKDFCDDP
     EANPRPSASG KFEFYSQVLA DTVNAMGYSE IKPIPTHIPP VEGYEATFKD WQGKIKGDYP
     YQVINPHYLR RSHTVFDNVQ WLRETWPNPV YISTQDAKEK GLADGDTVLL TSQHGKTLRT
     ACLTDRFMPG VIGLPHGSWV DMDEKTGIDT GGADNILCGP VSTGQGVSGW NSCVCNMEKY
     SGASLIADVQ KPQRIIL
//