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}.
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; 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
//