ID A0A0S8CL39_9BACT Unreviewed; 884 AA.
AC A0A0S8CL39;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=AMK69_15920 {ECO:0000313|EMBL:KPK24560.1};
OS Nitrospira bacterium SG8_3.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704023 {ECO:0000313|EMBL:KPK24560.1, ECO:0000313|Proteomes:UP000051394};
RN [1] {ECO:0000313|EMBL:KPK24560.1, ECO:0000313|Proteomes:UP000051394}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_3 {ECO:0000313|EMBL:KPK24560.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK24560.1}.
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DR EMBL; LJNR01000301; KPK24560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8CL39; -.
DR PATRIC; fig|1704023.3.peg.1782; -.
DR Proteomes; UP000051394; 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 Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 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 PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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.
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}.
FT DOMAIN 13..70
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 884 AA; 99885 MW; 2476375F03BBD244 CRC64;
MNSKAYTNAD IKDYWGYSVC SGCYNLCGVK IRVVDGVPVA IEGVPESDLG GQGGLCGRGV
ATIMDLHDPN RLQYPVKRTN PKKGLYEDPK WERISWEEAL GTITEKLKAA MEYDPRSIVW
SFTPGPGTPF KSTIYTSFFF LACGSLNQAF GGVGSQCGAA AHHAGALMHA AWDILPDYRY
CNFLLRCGGN EGHGGGRMAA TSMRQAAAAR DRGMRTVVMD PIGFRAGADA DEWIPILPAT
DIAVFLAMAN LIVHEIGIYD RDYIRHKTNG VYLVGPDMLF VRDKESGKPL IWDEKDSKAK
TYDDPSLSHP AMEGEYSVNG IKCHPAFHLW KEVIKQYDPE WASEVSTVPG ERIRRLAEEL
VENAKIGSTI EIGGKKFPYR PVAVVGYKGV QTHQNAFHQY LAMNLLNVLM GAQDVPGGVV
GSGTVRSFGH PESGRPQFEP YGGVDGMLTP GFWHTRTPWP PHDVTGPGMV NLLDIMADSS
MNPYPYTDDF DEIWTKIGRP YEVQVFGMYG GNVVMNIINE KTVDNFLGKI PFMFSINTTH
NETTEGFADI VLPDVHAYES YDIASSIGFF FNYPIGLDKW SFHLRMPVAE PMYDLKDTLD
IYFELADRVG IREKYNTFLE NYFSGKKSTW EQDDVTDTSY ILLKPDEKIK AKEFTDRVLK
YYFGEQKGLD WFEENGFITW EKRPEEAYWR YHVDARIPMY FETVARNKPK IKEIFENIGI
HMNWDYYTPL ISYFPSVIYT ELPEDSEFDL LGVSYRDTLH THRFFLENPM VDEMSASNPY
TFNIVMNEET AEKRNIQDGD LICVENHWGD KVEGRVKLSR LIHPRALAVV GLGGWAKGRP
IAKGKGVNFN SLLRADYKHM CPVVGSLEIV SRMKAYTVKR RTEQ
//
