ID A0A1F8MX86_9CHLR Unreviewed; 729 AA.
AC A0A1F8MX86;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=4Fe-4S Mo/W bis-MGD-type domain-containing protein {ECO:0000259|PROSITE:PS51669};
GN ORFNames=A2Y72_02680 {ECO:0000313|EMBL:OGO03238.1};
OS Chloroflexi bacterium RBG_13_53_26.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797629 {ECO:0000313|EMBL:OGO03238.1, ECO:0000313|Proteomes:UP000180304};
RN [1] {ECO:0000313|EMBL:OGO03238.1, ECO:0000313|Proteomes:UP000180304}
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 -!- 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:OGO03238.1}.
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DR EMBL; MGMW01000030; OGO03238.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8MX86; -.
DR Proteomes; UP000180304; 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; 3.40.50.740; -; 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 PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 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.
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 43..99
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 729 AA; 80344 MW; AE814228A59DEC03 CRC64;
MSRRAFLGIS AAAAAALTAI VVIKRPKPDE TLDKGTESAV ETEQFIFTSC LNCPTRCAIK
VRVVNGKAVR IFGNSNSPYS DGKTCPRSHV GLQVLYNPDR FTTTPLARVS GRAKGNGVDL
ENDFERISWD EAISRIAQKL GSISPEKLLM LQGLNTNSNE DLIRQFARAY GTTNLFHEES
LEMAADVEGK RMADGRDNSG YELRSENASE TSTKYILAFG ASIVESEKPL ARNIHLWGEL
RRGTPNGSKV VVIDPRYSVT AAKADQWIPI NPGTEGAMAM AMANVIIGED LIDHDFIDNW
TTGFENFKTV ATSYRFSPEE VAKITGVDAE VIRETAMDFA RSRPSVAWSG ESATSWAYGS
YASHAIFCLN ALVGSIDVPG GIVYQESPPY RPLPLDVTEG GISFRELADL VRNGSVEAAL
GFNSNLIMSV PSTKKWNDAL KNLPYYVHIG PAMNEMAAYA DIILPACTYL EEWGYESAIP
GSGYAEARIK QPVVSPLYES SAIATILYDL ATEMGSPVSD PFMAMGGSAV GFGEEFVRYR
TETFVSWEDF RRDGVWVGED YQYYKYDEIF HTPSDRFEFK STHLERLLNV SLPGEDTQRP
FMMGIYRPVM EMRSGVQNCP WAQEVFLVMD GIGWNNVVEM NREAAERMGI GDGDEVVVES
EFGEIEAEAR VRQGILPGAA AMATGQGRYA SGRWADDIGV NPNEVIGIEY DEESGQPSYF
STRVKIRKA
//
