ID   D6XU80_BACIE            Unreviewed;       857 AA.
AC   D6XU80;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ADH99366.1};
GN   OrderedLocusNames=Bsel_1861 {ECO:0000313|EMBL:ADH99366.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Salisediminibacterium.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99366.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH99366.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) 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}.
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DR   EMBL; CP001791; ADH99366.1; -; Genomic_DNA.
DR   RefSeq; WP_013172788.1; NC_014219.1.
DR   AlphaFoldDB; D6XU80; -.
DR   STRING; 439292.Bsel_1861; -.
DR   KEGG; bse:Bsel_1861; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_9; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
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   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; 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; IPR027467; MopterinOxRdtase_cofactor_BS.
DR   InterPro; IPR006311; TAT_signal.
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; 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   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          54..115
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   REGION          84..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  95152 MW;  1565F68BC166A1B8 CRC64;
     MFELFNRVKA FKISRRAFIG TGAAVTAGAV LPASANGLKK LSAVQAESLQ QEEGEWIPAA
     CWHNCGGRCL LKAQVVDGVV KRVKTDDTRE DSPDNPQQRA CVRGRSQRQQ VYGVDRLKYP
     MKRKHWEPGG GDKSRRGEDE WERISWDEAT DIIASEIKRI KNQYDNRSIL VTGGDIGRAL
     NLVGGHVSTW GTTSWGSWRW GPAYFGLQEG YFEHSINDRM DLRNSQLIVL WGMNPAWSSP
     GSPTYNFLQA KKAGARFIVI DPMYSESAEL LGDEWIPVHP GTDHALMLGM AHTIITEDDP
     DQNPLIDWDF LKSCTVGFDE SMMPEGSDSK QNFKDYVLGI HDGEPKDAEW ASSISGVDVT
     MIKRIAREIA TTNRAALLTG WAPARIKNSD SWPQMFMTFG AMTGHMAQAG RMTGVSCHFG
     TGNGGPRLVN GGGAGVPPSA ENPVEDSLVH AEMWKAIKEG EYTAGYNDKR DINIQMIYHG
     MGATLQTRDG QANGIDVHKE VEFVVTNGHF ITTNAKYSDI VLPATTHWER EGGFNTGNRD
     ALFYYRRVIE PMFEAKDDAE ITTMIGEKLG FSAEEVYGDV SARQQLFNQI AGATVINEAG
     TDFEPLVTIT KDDLSEWGVE GQTQQGRISI QELEEKGVYQ VERKPGDNYG YIAQEAFRQD
     PEANPLATAT GKLEIYSEAL QEYVKSIGFT EIDPIPTYNP AIEGYEETYS NFNSREKGDL
     PLQVINPHYL RRAHTIFDNN PWLREAWPNH VYVASADADE RGVKDGDTVK VTSKHGSTLR
     IAHVTERLMP GTVGLMHGAW VEIDPETGID RAGSDNILTG SIATGQAISG WNSTIADFEK
     WEGIPLKEDK HWELRTV
//