ID A0A1G9X5T8_9BACI Unreviewed; 663 AA.
AC A0A1G9X5T8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Anaerobic selenocysteine-containing dehydrogenase {ECO:0000313|EMBL:SDM92047.1};
GN ORFNames=SAMN05443253_106280 {ECO:0000313|EMBL:SDM92047.1};
OS Bacillus sp. OK048.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1882761 {ECO:0000313|EMBL:SDM92047.1, ECO:0000313|Proteomes:UP000199133};
RN [1] {ECO:0000313|EMBL:SDM92047.1, ECO:0000313|Proteomes:UP000199133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK048 {ECO:0000313|EMBL:SDM92047.1,
RC ECO:0000313|Proteomes:UP000199133};
RA de Groot N.N.;
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 -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FNHN01000006; SDM92047.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9X5T8; -.
DR STRING; 1882761.SAMN05443253_106280; -.
DR OrthoDB; 219031at2; -.
DR Proteomes; UP000199133; 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:InterPro.
DR CDD; cd02766; MopB_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; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000199133}.
FT DOMAIN 3..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 663 AA; 74983 MW; 791A23EDAE04165E CRC64;
MKEAIYRNTC PRNCYGTCGI LSHVKNGKLI KVTGDPDHGY SKGRLCAKGY AYTEYVYSPN
RLKYPMLQSP RGSGNWKRIS WDEAYTIIAS KMVELNQRYG SNLASGYNKY SGNLGLLHYA
TEGMFNSMGP HTMPIGNPCA LTGRLAMNRS FGENYSSIPE DMAGAKLIVL WGANPAITNV
HQMKFIYEAR KQGAKLVVID PVFSQTAQKA DLYIQIHPGT DQLLAHGIAK LVINRKQHCI
QFLEKQTEGW LEYKQYLENH LSIQEVCRQT GVSIEALREL SELYGTTKPI ATWAGLGVQR
NKRGSESISA INSLAAVTGN LFIPNGGLYY MHFDVEDFPC ALLNHKGPEH PSIPASREVD
ISDYAANALL LSDPPLKLLW IASRNITQDQ NFNAWDELFQ QIELIVTVDL YMTKTAERSD
IVLPAATHFE EEDLNVGYWH YWLSFNQKAI PPYYEAKSDL QIARELTTKL NELSPGFSNF
PASKEPIDWI KEELTPEIME LYSFSSFEEL MERPFKKDIT KVMSEDRNKF RLFSPANQRA
HDQAGFDKAN EYKLITPQSL LKIHSQYESL NWLNSPQDES CIELSIEAAR VNGIKEREKI
EVYNDQGKIV GVSKINPHLP KTIILAHQAG DHPINQLISQ PNDQIGSTYF YDSMVKIKKA
EAP
//
