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Entry: S5MSY1_SALBN
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ID   S5MSY1_SALBN            Unreviewed;       801 AA.
AC   S5MSY1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:AGR59826.1};
GN   ORFNames=A464_2641 {ECO:0000313|EMBL:AGR59826.1};
OS   Salmonella bongori N268-08.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1197719 {ECO:0000313|EMBL:AGR59826.1, ECO:0000313|Proteomes:UP000015042};
RN   [1] {ECO:0000313|EMBL:AGR59826.1, ECO:0000313|Proteomes:UP000015042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N268-08 {ECO:0000313|EMBL:AGR59826.1,
RC   ECO:0000313|Proteomes:UP000015042};
RA   Marti R., Hagens S., Loessner M.J., Klumpp J.;
RT   "Genome sequence of Salmonella bongori N268-08 - a rare clinical isolate.";
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP006608; AGR59826.1; -; Genomic_DNA.
DR   AlphaFoldDB; S5MSY1; -.
DR   KEGG; sbz:A464_2641; -.
DR   PATRIC; fig|1197719.3.peg.2635; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   Proteomes; UP000015042; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0009389; F:dimethyl sulfoxide reductase activity; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   CDD; cd02794; MopB_CT_DmsA-EC; 1.
DR   CDD; cd02770; MopB_DmsA-EC; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.12440; -; 2.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR   InterPro; IPR011888; Anaer_DMSO_reductase.
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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR   InterPro; IPR006311; TAT_signal.
DR   NCBIfam; TIGR02166; dmsA_ynfE; 1.
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; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR   PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 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   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          62..123
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   801 AA;  88953 MW;  A05089FEF8132CDE CRC64;
     MRFYLQSRIM KKIKSQGNGD QPAISRRNFI QASSALIALP FISSTGTARA RTAPAAENMS
     TETVVQTCST FDCGGKCDIR AHVSEGIVTR ISTRPDNALD PQMPVMRACV RGRAYRKFVY
     HPDRLKYPMK RVGKRGEGKF ERISWDEATT LIANNLTSIT EKYGPASRYV HVGTAVSGGT
     FSGDKMVRRL LNLTGGYLES YHSVSMGNTA AATPYTYGTA ASGSSLDTLL DTKLVILWGH
     NPTETIFGHT NYFFQQMKQN GTRFIVVDPR YSDTVASLAD QWIPLLPTTD NALMDAMMYV
     IISENLHDRA FIERYAIGFD EASMPEGVPA NESLVAYLTG AKDGVVKTPE WAEKITHVPA
     QTIRQLARDY ANTKPAALIQ GWGPQRHNCG ERTARGSTLL ATITGNVGVK GGWAAGYGGC
     PNRKFAAGPE MPDNPVKAKI SVMNWVQAAD DASLVTPEVG LKEANKLDSN IRILFSLAGN
     YLANQNPDLH QAVRVLEDES KIQFIVASDL FMTPSAKYAD LLLPETSFME RWNIGETWGT
     ANYLILSEKL IEPEFERRSD YDWLREVAAK LGIEDDFSQG RDEKAWIEHI WEQTRLAMPD
     ENLPDFATLQ KTRQHLFKSA PFVAFEDNIR DPENHPFPTP SGKIEIFSKR LYDMKHPEIP
     ALSHYVPAHE GPEDALVKDF PLQLITWKGK NRANSTQYAN PWLIEVQQQK VWINPQDAQK
     RGITQGDMVR IHNQRGICEI PAEVTPRVIP GVVAMQAGAW WQPDENGVDK GGCANVLSSA
     RITALAKGNS HQTMLVEVAK A
//
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