ID   A0A368VKS5_9BACL        Unreviewed;       687 AA.
AC   A0A368VKS5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Anaerobic selenocysteine-containing dehydrogenase {ECO:0000313|EMBL:RCW42309.1};
GN   ORFNames=DFP97_11732 {ECO:0000313|EMBL:RCW42309.1};
OS   Paenibacillus prosopidis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=630520 {ECO:0000313|EMBL:RCW42309.1, ECO:0000313|Proteomes:UP000252415};
RN   [1] {ECO:0000313|EMBL:RCW42309.1, ECO:0000313|Proteomes:UP000252415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7506 {ECO:0000313|EMBL:RCW42309.1,
RC   ECO:0000313|Proteomes:UP000252415};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (JUL-2018) 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}.
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:RCW42309.1}.
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DR   EMBL; QPJD01000017; RCW42309.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368VKS5; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000252415; 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   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; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
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:UP000252415}.
FT   DOMAIN          7..64
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   687 AA;  77094 MW;  58D6D6459FF13B27 CRC64;
     MTKSVKSGTF RSVCPFDCPD TCGLSVTMDE GIITKITGDN EHPVTRGAIC NKVRQLSDRI
     YHPERLLYPM RRTGPKGTLA FKRISWDEAY EEITDRMRNI IHEHGANAIL PYSFYGNMGV
     LNAEGMDRRF FHRLGSSRLD RTICNAAGAA GYKYTMGGSI GIDPEETVHT KLFLIWGCNL
     VSTNMHQAML ATEARKNGAT IIHIDVHRNR TSAWADRFIH VRPGTDAALA LGMMHVIIRD
     GLSDIAFLEQ HAIGYEELAE QAADYTPERV ADITGVPAAE IEELARLYGT TSPSFIRIGN
     GLQHHDNGGM IIRTISCLPA LTGQWGIRGG GAMKGNSWYS RLNGERIERP DLLPDPNVRT
     INMNQLGDAL LDLDPPVRML FVYNSNPAIV APDQNRVREG LLRDDLFTVT HDLFLTDTCK
     YSDIVLPATS HFENMDLYTS YWHLYLQLHE PIIQPMGECI SNFTLFKQLA LRLGFERETF
     DISEKQMIQE ALDSDQNPYL AGITFEQLIG RTWMKAGGDN LPPFTDRIPT RSGKIELCSE
     TMLRDGLPPL PDHIPLREPD KYPFWLMTGP NHSFINSTFA NQERLQKLEK EPLLYIHADD
     ASELGMTNGE RVKIRNDRGE AEVILRIGTD VLPGVLVTQG LWWDDDRKGI QAVNALTSQR
     LADMGGGATF FSNRVEVLKI DTKDISD
//