ID A0A1V4M7X8_9FIRM Unreviewed; 668 AA.
AC A0A1V4M7X8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=AVO34_09490 {ECO:0000313|EMBL:OPL10846.1};
OS Firmicutes bacterium ML8_F2.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1775675 {ECO:0000313|EMBL:OPL10846.1, ECO:0000313|Proteomes:UP000189969};
RN [1] {ECO:0000313|EMBL:OPL10846.1, ECO:0000313|Proteomes:UP000189969}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ML8_F2 {ECO:0000313|EMBL:OPL10846.1};
RA Hamilton T.L., Pearson A., Macalady J.;
RT "Carbon and sulfur cycling below the chemocline in a meromictic lake.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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:OPL10846.1}.
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DR EMBL; LQBG01000069; OPL10846.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4M7X8; -.
DR Proteomes; UP000189969; 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 CDD; cd02766; MopB_3; 1.
DR CDD; cd02775; MopB_CT; 1.
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 InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 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; PS00490; MOLYBDOPTERIN_PROK_2; 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 3..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 668 AA; 73766 MW; 9416BECECC4B401A CRC64;
MLIKTIKTTC PLDCWDQCAM LVEVEKGRLL SISPDPEQKI TGKYLCRKGR QNLARLNHPD
RLRYPLLKKN GSFKRIGWNE ALQAMACHLS DALARFGPLS LLHYHDGGYG GLLKNLESRF
FSALGGCTEH RGSLCWAAGL AAQRYDFGEV YSHPHEDLAN ARLIIIWGRN PAHTQPHLLP
FIRQAQKKGA RVILIDPLRT ATAALADEYI RVKPGSDGAL ALGMAAMIIE KGLLDRDFIA
TASSGFERYR TMAAAFSLNK TASLTGLAPE VIENLAVDYA TAKPAALVIG IGLQRHSNGG
NTVRAVDALA ALTGNIGVRG GGASYANFQI SRLVDDSFLN GEDLQPIRRR YPKPGLAKAI
SEFSDPPVDF LYISRANPLT QVGDSDGLRR AFKRVPFVVT AEHFMTDTAN ASDLVLPATA
FLETEDLFYN SMSHQYLVYS AKCIEPPAEC RPEYVYLRDL ALLLDKEGFP APEPDRLLAR
AIEPLTNKTG VTLEEIRENS PYLLPGGNDI PWAGRVFETA DGRYNFYSPT AENDGVGGLP
VYREPVELGD KKLRREGYCY WFVTPHHRDS IHSSHRLPDG EVTPKAYLHP RTAEQEGLKG
GEKITVWSKR GCLQAVATVS DRVPPDAVVV YEGWWYESGA AVNKLTPART TDMGCQAAFY
DCLCRIEK
//
