ID A0A1F8N4P8_9CHLR Unreviewed; 743 AA.
AC A0A1F8N4P8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-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=A2Y60_06100 {ECO:0000313|EMBL:OGO05826.1};
OS Chloroflexi bacterium RBG_13_54_9.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797631 {ECO:0000313|EMBL:OGO05826.1, ECO:0000313|Proteomes:UP000180318};
RN [1] {ECO:0000313|EMBL:OGO05826.1, ECO:0000313|Proteomes:UP000180318}
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:OGO05826.1}.
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DR EMBL; MGMY01000027; OGO05826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8N4P8; -.
DR Proteomes; UP000180318; 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 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 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; PS00932; MOLYBDOPTERIN_PROK_3; 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..69
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 743 AA; 82358 MW; 9BACD2075C3DA9A9 CRC64;
MSAENAKFGG LGEQVIPTTC SSHCAATCLL KVHVKDGVIT RIETDDGDHP QLRACLKGRA
YRQRVYDPNR ILYPLKRVGK RGEGKFERIS WDEALGTIAE RLKTLRKTYG PESVLYAQMP
GDYGVLSFWG PMERLLNLSG GYTMFWGAAS LNGALYADIF TYGTLETANT IDDLLNSRLI
ILWACNAAVT VNGCNTSWYL AQAREAGTRI IVIDPRYTDT AATFADQWIP IIPGTDTAML
IAMAHVIIKE KLYNEKFLNT YTVGFPQFKD YVMGVEDGVP KTPAWAQEIT GVSSVIIEDV
ARQYATIKPA ALLASTAPGR TAYGEQYHRA TSTLAAMTGN IGIHGGWAAG GFPLGIASGF
PYVLPPMIAG IELYNFTPNL AQEKFPGRPQ GIFADLALGR QPQVHLNKYA DAILTGKAGG
YPADYKLLYI KKCNLLNSIA NVNKMVKALQ SGSLEFIVVE EQVMTATAKF ADIILPVNTY
MEREDMAYGD GLSFIGKQNK VIEPLGESKS PLQIAADLAE RMGIEGFLEK SPEEMLRERA
QMNDIHDFDQ WSKEGIHWLK LSEPHVAFKK QIEDPENNPF PTPSGKIEIY SQQIADMGDP
EAPPIPKYIQ TWESRNDTLA RKYPLQLITS HFKRRTNAQY DSVPWLRELQ EQRVMMNSVD
ARARGINDGD LVRVFNDRGE MMIRAWVTER IVPGVVDIPT GAWYKPDEKG MDTGGCANVL
TRDAYSPGGA FPYNTGLVEV QKV
//