ID   A0A1G0R8P9_9BACT        Unreviewed;       799 AA.
AC   A0A1G0R8P9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN   ORFNames=A2V66_05885 {ECO:0000313|EMBL:OGU56491.1};
OS   Ignavibacteria bacterium RBG_13_36_8.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798432 {ECO:0000313|EMBL:OGU56491.1, ECO:0000313|Proteomes:UP000177879};
RN   [1] {ECO:0000313|EMBL:OGU56491.1, ECO:0000313|Proteomes:UP000177879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGU56491.1}.
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DR   EMBL; MHAE01000107; OGU56491.1; -; Genomic_DNA.
DR   Proteomes; UP000177879; Unassembled WGS sequence.
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; 3.40.50.12440; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
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; IPR006655; Mopterin_OxRdtase_prok_CS.
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; PS00490; MOLYBDOPTERIN_PROK_2; 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..116
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   799 AA;  90638 MW;  C7D911024AD823AD CRC64;
     MNKNSQDEKD RLSMNRRDFI KWTTITGCSV IAVGSLDKVV EAVEQKTKPF LFAEKIIRTG
     CPAHNCGGKC LLKVHVKDGK IIRIETDDRP TDSIEDPQLR ACIRGRSYRR RQYHPDRLKY
     PMKRVGKRGE GNFERISWDE ALDKVVAEIK RVKEKYGNSA IYVPYGTGSY NQTNGRQTAY
     RLMNLYGGSL GFYNSYSWAA ISKATPYVFG TSVTGNQRQD WINSKYIIMW SWNPCEMRDG
     TNSEFFLKKA KENGAKIICI DPRMSMSAVA LADEWIPIRP GTDVAMMSAM AYVMVTENLY
     DKDFVKKYCV GFDKTQMPKG AEDAESYKDY ILGVLDGVPK TPQWAESITT VPKETIVRIA
     RNYATIKPAM LYQGYGMQRR AYGEQAVIGG CVLASMTGNI GIPGGCASGL ALQADDGGPF
     WNVFPTSTNS VKARIPTFLW TEAVLRGKEM TSKEGVTGVD KLDNNIKLIX XXATNALINQ
     HANVNRTAKI MADENLVEFI VVHEQFLTST AKFTDILLPV CTQFEVYGLE DGWKYGDEVI
     LMPKIVEPYY ETKSDYQICS EVAERLGIKK EYTEGRSERD WIEWSLEQYR QTRFPDVPSL
     DKFEKSNTGV YSLPITKPKI AFEDFRKDPV KNRLNTPSGK IEIFSKTLYD MNNPEFIPPI
     PKYLQEWESP FGSEAEKYPL QAVGHHYMSR VHSTHDNNDW TNEAFPQRVF INPIDAEKRG
     IDDGDEVKIF NGRGVMIIPC RVTKKIMPGV IDIPQGAWWM PDENGIDRRG CVNVLTSEKW
     TPLAFGNAQH TIMVQVERV
//