ID A0A0S8EFK0_9CHLR Unreviewed; 190 AA.
AC A0A0S8EFK0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=AMJ77_03640 {ECO:0000313|EMBL:KPK47272.1};
OS Dehalococcoidia bacterium SM23_28_2.
OC Bacteria; Chloroflexota; Dehalococcoidia.
OX NCBI_TaxID=1703396 {ECO:0000313|EMBL:KPK47272.1, ECO:0000313|Proteomes:UP000054036};
RN [1] {ECO:0000313|EMBL:KPK47272.1, ECO:0000313|Proteomes:UP000054036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_28_2 {ECO:0000313|EMBL:KPK47272.1};
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 -!- 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}.
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:KPK47272.1}.
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DR EMBL; LJUA01000032; KPK47272.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8EFK0; -.
DR STRING; 1703396.AMJ77_03640; -.
DR PATRIC; fig|1703396.3.peg.1446; -.
DR Proteomes; UP000054036; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..190
FT /note="4Fe-4S Mo/W bis-MGD-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006645116"
FT DOMAIN 41..98
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 190 AA; 20684 MW; E69DF51C46900B19 CRC64;
MTKLSRRHFL VLCAATNAGL LLPTGSAAAK GVGDFPLHKK VGESHTICPY CSCGCGLVIA
TDENGHITNA EGDPDHITNR GALDPKSISV PQLSNSPLRL HTVMYRAPNS EQWEEKSWDW
AVKEIANRIK KTRDETFVTT TKVDGKDVAV NRTEGLAWIG GAANNSEDCY LSTKLARALG
IVYLEHQARI
//
