ID C9Y3U7_CROTZ Unreviewed; 794 AA.
AC C9Y3U7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:CBA30747.1};
DE EC=1.7.2.3 {ECO:0000313|EMBL:CBA30747.1};
DE EC=1.7.99.4 {ECO:0000313|EMBL:CBA30747.1};
GN Name=dmsA {ECO:0000313|EMBL:CBA30747.1};
GN OrderedLocusNames=Ctu_20690 {ECO:0000313|EMBL:CBA30747.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA30747.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(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}.
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DR EMBL; FN543093; CBA30747.1; -; Genomic_DNA.
DR AlphaFoldDB; C9Y3U7; -.
DR KEGG; ctu:CTU_20690; -.
DR PATRIC; fig|693216.3.peg.1954; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000002069; 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 GO; GO:0008940; F:nitrate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
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 ECO:0000313|EMBL:CBA30747.1}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 52..113
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 794 AA; 88070 MW; 5128DC9D5C1E2D06 CRC64;
MKPLTQKDGP GEGGLTRRDF LRATSALAAA PLFVQAGTAN ADEPEVQPQA AEKIVPTCST
FDCGGKCDIR AHVREGVVTR ISTCPDNEVD PAMPLMRACV RGRGYRQFVY HPDRLKYPMK
RVGKRGEGQF ERISWDEATT LIADNLRRIT AKYGPASRFM HTDTAVSGGA FSGDKMARRL
LNMTGGYLES YHSVSMGNTA AATPYTYGTA ASGSSLDTLS DTKLVILWGH NPNETIFGHT
NHYFQQMKRN GTRFIVVDPR YSDTVASLAD QWVPLLPTTD NALMDAMMFV IISENLHDSA
FIARHVIGFD ENTMPEGVPA GESLMAYLFG EKDGVKKTPE WAERITHVPA QTIRQLARDY
ATTRPAALIQ GWGPQRHICG ERTARGSTLL ATITGNVGVK GGWAAGYGGI GNRLFCADPY
SVPNPVTAKI SIMNWVQACD DAAKVTPDNG LKDAETLSSN IKFIFNLAGN YLANQNPDIN
QTVKVLEDES KVEFIVVSDL FLTPSARYAD LLLPETSFME RWNIGETWGT GNYLLLSQKL
VEPEFERRSD YDWLRDVARK LGIEARFSEG RSEKEWIAHI WEKTREALAD HDLPDFAGLC
RNPHVYLKSP PYVAFEENIR DPDNHPFPTP SGKIELFSKR LWEMQHPEIP ALSHYVPAQE
GPQDTLRAKY PLQLITWKGK NRANSTQYAN PWLQEVQRQQ LWINPQDAQA RGIQQGDSVR
IYNDRGVVQI PAEVTPRVMP GVVAMQAGAW WQPDADGVDN GGCPNVLTSA RITPLAKGNA
HQTLLVEVTK HASV
//
