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Database: UniProt
Entry: A0A1Q7I1X5_9CHLR
LinkDB: A0A1Q7I1X5_9CHLR
Original site: A0A1Q7I1X5_9CHLR 
ID   A0A1Q7I1X5_9CHLR        Unreviewed;       195 AA.
AC   A0A1Q7I1X5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN   ORFNames=AUH85_02775 {ECO:0000313|EMBL:OLC57611.1};
OS   Chloroflexi bacterium 13_1_40CM_4_68_4.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1805077 {ECO:0000313|EMBL:OLC57611.1, ECO:0000313|Proteomes:UP000185706};
RN   [1] {ECO:0000313|EMBL:OLC57611.1, ECO:0000313|Proteomes:UP000185706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27843720;
RA   Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA   Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA   Banfield J.F.;
RT   "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT   heterotrophy are prevalent below the grass root zone.";
RL   PeerJ 4:E2687-E2687(2016).
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:OLC57611.1}.
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DR   EMBL; MNFM01000031; OLC57611.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q7I1X5; -.
DR   Proteomes; UP000185706; 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}.
FT   DOMAIN          46..106
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   195 AA;  20707 MW;  7BBE9480C092BFEB CRC64;
     MAVTRRQLLK MTGIGSAGVA ATSLGALGFD LAFATDRAAK YKLEGVTATP SICPYCAVGC
     GTLVQTRDDG NGRQIINIEG NPDSPISTGS LCPKGAATFQ LAMNPKRISQ VQRRAPGSDK
     WETMSLDAAM ARITELVATS RDATFVEKTS DGKLINQATG IFALGGATND NEENYLICKV
     MRMMGVVRIE NQARI
//
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