ID A0A0M2WRE7_9BURK Unreviewed; 691 AA.
AC A0A0M2WRE7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Dimethyl sulfoxide reductase DmsA {ECO:0000313|EMBL:KKO63818.1};
DE EC=1.8.5.3 {ECO:0000313|EMBL:KKO63818.1};
GN Name=dmsA {ECO:0000313|EMBL:KKO63818.1};
GN ORFNames=VM94_03571 {ECO:0000313|EMBL:KKO63818.1};
OS Janthinobacterium sp. KBS0711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO63818.1, ECO:0000313|Proteomes:UP000034315};
RN [1] {ECO:0000313|EMBL:KKO63818.1, ECO:0000313|Proteomes:UP000034315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KBS0711 {ECO:0000313|EMBL:KKO63818.1,
RC ECO:0000313|Proteomes:UP000034315};
RA Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKO63818.1}.
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; LBCO01000024; KKO63818.1; -; Genomic_DNA.
DR RefSeq; WP_046684553.1; NZ_VCCE02000001.1.
DR AlphaFoldDB; A0A0M2WRE7; -.
DR PATRIC; fig|1649647.5.peg.3659; -.
DR Proteomes; UP000034315; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02766; MopB_3; 1.
DR CDD; cd02786; MopB_CT_3; 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 Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
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; IPR037920; YoaE_C.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 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.
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 Oxidoreductase {ECO:0000313|EMBL:KKO63818.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000034315}.
FT DOMAIN 3..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 691 AA; 74806 MW; 84D4FF5BE742D3FE CRC64;
MTTTQVRAAC PLDCPDTCAL LVTVTDGVAT AVKGDPDHPT TAGVLCTKVS RFTERTYHAD
RLLHPLRRVG KKGEGKFERI SWEEALQTIA ARLKPIAARD PQAILPYSYC GTMGLVQGES
MSSRFFNQLG ASLLDRTICA SAGATGYRYT VGASIGTDME QFQNAKLIII WGGNPIASNL
HFWMRAQEAK RNGATLIAID PYRSLTAEKC HQHIALLPGT DAALALGLMH VLITEDLLDH
DYIAQYTIGY AELKQRALEW PPERVAEVCG ITATEVVELA RLYGQACRSG EGAAIRANYG
VQRVHGGGMA VRNIACLPAL TGAWRHPAGG MQLSSSGSFP VNRKALQRPD LLKGTPRTIN
MSTIGDDLLK ESSAEFGPQV EAVIVYNSNP LAVAPDSSKV AQGFAREDLF TVVLEHFQTD
TVDYADIVLP ATTQLEHVDA HSTYGHLYMM ANNAAVAPLG EAKANTEIFR LLAQHMGFDD
PCFQESDDAL AAKAFDTTDA RAVHFDWESL KRTGWQKLAM AEAPFATGGF PTPSGKCELY
SSAMAQAGLD PLPTYIAPHE SQASNPALAA RYPLAMISPP ARNFLNSTFV NVKSLRAAEG
EPHLDIHPDD CATRGIAAGD MVRIFNDRGS FVAKARVTDK ARRGLVVGLS VWWKKLASDG
KNANEVTSQR LTDMGRAPTF YDTLVEVEKA A
//
