ID B5F1A5_SALA4 Unreviewed; 792 AA.
AC B5F1A5;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain a {ECO:0000313|EMBL:ACH49167.1};
DE EC=1.8.99.- {ECO:0000313|EMBL:ACH49167.1};
GN OrderedLocusNames=SeAg_B2682 {ECO:0000313|EMBL:ACH49167.1};
OS Salmonella agona (strain SL483).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454166 {ECO:0000313|EMBL:ACH49167.1, ECO:0000313|Proteomes:UP000008819};
RN [1] {ECO:0000313|EMBL:ACH49167.1, ECO:0000313|Proteomes:UP000008819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL483 {ECO:0000313|EMBL:ACH49167.1,
RC ECO:0000313|Proteomes:UP000008819};
RX PubMed=21602358; DOI=10.1128/JB.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001138; ACH49167.1; -; Genomic_DNA.
DR AlphaFoldDB; B5F1A5; -.
DR KEGG; sea:SeAg_B2682; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000008819; 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; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; 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 ECO:0000313|EMBL:ACH49167.1}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 53..114
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 792 AA; 87725 MW; D9587F73DAF70ED8 CRC64;
MKNIKSQGNG EQPAISRRHF IQASSALIAL PFVSSPATAQ ARAVTATENR PAEKVVQTCS
TFDCGGKCDI RAHVSDGIVT RISTRPDNAL DAQMPVMRAC VRGRAYRKFV YHPDRLKYPM
KRVGKRGEGK FERISWDEAT TLIADNLKSI TEKYGPASRY VHVGTAVSGG TFSGDKMARR
LLNLTGGYLE SYHSVSMGNT AAATPYTYGI AASGSSLDTL LETKLVILWG HNPTETIFGH
TNYFLQKMKQ NGTRFIVVDP RYSDTVSSLA DQWIPLLPTT DNALMDAMMY VIISENLHDR
AFIARYAIGF DEDSMPEGVP ANESLVAYLT GAKDGVVKSP EWAEKITHVP AQTIRQLARD
YANTKPAALI QGWGPQRHNC GERTARGSTL LATITGNVGI KGGWAAGYGG CANRKFAAGP
EMPDNPVKAK ISVMNWVQAA DDASKVTPDM GLKDADKLDS NIRILFSLAG NYLANQNPDL
HQAVRVLEDE SKIQFIVASD LFMTPSAKYA DLLLPETSFM ERWNIGETWG TASYLILSEK
LIEPEFERRS DYDWLREVAA KLGIENEFSQ GRDEKAWIEH IWEQTRLAMP DENLPDFATL
QKTRQHLFKS APFIAFEDNI RDPENHPFPT PSGKIEIFSK RLYDMQHPEI PALSHYVPAH
EGPEDALAKD FPLQLITWKG KNRANSTQYA NPWLIEVQHQ TLWINPQDAQ KRGITHGDMV
RIHNSRGICE IPAEVTPRII PGVVAMQAGA WWQPDENGID KGGCANVLSS ARITALAKGN
SHQTMLVEVA KA
//
