ID N0AY46_9BACI Unreviewed; 780 AA.
AC N0AY46;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE {ECO:0000313|EMBL:AGK55578.1};
GN ORFNames=B1NLA3E_19170 {ECO:0000313|EMBL:AGK55578.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK55578.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK55578.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK55578.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
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; CP005586; AGK55578.1; -; Genomic_DNA.
DR RefSeq; WP_015595620.1; NC_021171.1.
DR AlphaFoldDB; N0AY46; -.
DR STRING; 666686.B1NLA3E_19170; -.
DR KEGG; baci:B1NLA3E_19170; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000013300; 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 Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
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; 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; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000013300};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 45..105
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 780 AA; 86736 MW; EEC81745F1B7AB26 CRC64;
MSIKLDRRTF LKLSGSVAGT VAVSGTWEVL TKEQLASAVN TDEGTQVIPV LCNHNCGGRC
QIKAHVKDGV VVRITTDDRP DLENNPQLRA CLKGRATRNR VYHPDRLKYP MKRVGKRGEG
KFERITWDEA TDLIAKNLKK IVDQYGPHSV YVNYATGDEG AMAGRTSAKR LMNMMGGYLG
YYGSYSSACL KYTAPFVTGY RDTNSYQTLH HSKLIILSGF NPAETVFETN SNYYLAKAKK
AGAKVIVIDP RYTESAATFG DQWIPIVPST DTALFSAMAY VIITENLHDQ AFLDKYTIGF
DEEHMPEGVP SGNSYKSYIL GTTDGQTKTP EWAAAITGID ANTIKNLARE YATTKPAQLL
QGLGPQRHAQ GESSVRAGIV LAAMTGNIGI LGGGWGGGEG GRKLGLDVGE LPTGDNPVET
QISVFMWTDA VVRGTEMTEK DGVQNGPLKS NLKFMWNLGS NTLVNQHADI NKTIKILEDE
SKLEYIVVSE QFMTPSAKFA DILLPSDHAF ERYDFGFPWT GENYILFGNK VIEPPGECKH
DYWWMSKVAE KLGLGEKFTE GKTQEDWMKQ LVADAQKADP QFPSWEELKK KGLYRSDARE
YVSYEKEIKD PANNPFQTPS GKIEIFSKTL FDMKNDEIPG VPKYTPAAEG PEDSLREKYP
LQCFGPHIKR RTHSTWDETP WMEEAEPQQM WINPEDAQAR GLQDGDKAKV YNDRGALVIP
VRITKRIRPG VVSIPQGAWY TPDDKGVCQR GCINILTSQR PTPLAHGNGQ HTNLVQVKKL
//
