ID A0A1V3JV03_9PAST Unreviewed; 806 AA.
AC A0A1V3JV03;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dimethyl sulfoxide reductase subunit A {ECO:0000313|EMBL:OOF60158.1};
GN ORFNames=BKL49_00230 {ECO:0000313|EMBL:OOF60158.1};
OS Rodentibacter myodis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Rodentibacter.
OX NCBI_TaxID=1907939 {ECO:0000313|EMBL:OOF60158.1, ECO:0000313|Proteomes:UP000188602};
RN [1] {ECO:0000313|EMBL:OOF60158.1, ECO:0000313|Proteomes:UP000188602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac151 {ECO:0000313|EMBL:OOF60158.1,
RC ECO:0000313|Proteomes:UP000188602};
RA Christensen H.;
RT "Rodentibacter gen. nov. and new species.";
RL Submitted (OCT-2016) 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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOF60158.1}.
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DR EMBL; MLHQ01000001; OOF60158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V3JV03; -.
DR STRING; 1907939.BKL49_00230; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000188602; Unassembled WGS sequence.
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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR02166; dmsA_ynfE; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 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; PS00551; MOLYBDOPTERIN_PROK_1; 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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..806
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011985208"
FT DOMAIN 47..109
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 786..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 806 AA; 90153 MW; 2EFD526DF7671780 CRC64;
MSNANQISRR NFIKASSVGA AVAVSNLSLP FSAVAAETST TPKDGEEKIV WSACTVNCGS
RCPLRMHVKD NRITYVETDN TGTETYNLDH QVRACLRGRS MRRRVYNPDR LKYPMKRVGK
RGEGKFKRIS WDEALTEIAR ALKRNIEKYG NESIYLNYGT GTLGGTMTKS WPPASTMVAR
FMNCIGGYLN HYGDYSTAQI AVGLDYTYGG GWAMGNGMAD IENTKLIVLF GNNPAETRMS
GGGLTYCIEQ AKARSNAKMI IIDPRYNDTA AGREDEWIPI RPGTDAALVS ALAYVMISEN
LVDQPFLDKY CVGYDEKTLP KDAPKNGHYK AYILGMGEDG IAKTPEWAAK ITGIPADRII
KLAREIGSTK PAFIAQGWGP QRRSNGELIS RAIAMLPILT GNVGIHGGNT GARESAYSIP
FVRMPTLENP VQASIPMFMW TDAIIRGSEM TALTDGIRGV DKLSSPIKVI WNYASNCLIN
QHAQINRTHE ILQDESQCEM IITIDNHMTS TAKYSDILLP DCTASEQMDF ALDAYVANMN
YVIFADQVIK PSFECRNIYD MLSDLAEKMG VKEKFTEGRT QEQWLRHIYE QSREQLPELP
TFDEFRQQGI FKKVDPNGFY VAYKDFREDP EKNPLQTPSG KIEIYSSRLA EIAKTWKLAE
DEVIHPLPIH AQSFEHYGDP LMEKYPLQLS GFHYKARTHS TYGNVDVLKA ANPQEVWMNP
IDAQPRGIKN GEMIRIFNDR GEVRINVKVT PRIMPGVVAL SEGAWYAPDK DRIDHSGCIN
VLTTQRPSPL AKGNPQHSNL VQVERL
//
