ID A0A0F2PIM6_9FIRM Unreviewed; 694 AA.
AC A0A0F2PIM6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:KJS12372.1};
GN ORFNames=VR67_09265 {ECO:0000313|EMBL:KJS12372.1};
OS Peptococcaceae bacterium BRH_c8a.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX NCBI_TaxID=1629715 {ECO:0000313|EMBL:KJS12372.1, ECO:0000313|Proteomes:UP000033493};
RN [1] {ECO:0000313|EMBL:KJS12372.1, ECO:0000313|Proteomes:UP000033493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c8a {ECO:0000313|EMBL:KJS12372.1};
RA Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (MAR-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:KJS12372.1}.
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DR EMBL; LADP01000021; KJS12372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F2PIM6; -.
DR STRING; 1629715.VR67_09265; -.
DR PATRIC; fig|1629715.3.peg.4189; -.
DR Proteomes; UP000033493; 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; cd02778; MopB_CT_Thiosulfate-R-like; 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 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 1..56
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 694 AA; 76952 MW; 261B544337D43801 CRC64;
MSVYSICLMC TVRCPIKVEI ENNDVRLIEG NPHAPGIEGS ICPKGAAGVA LLNDDQRLKK
PLIRTGPRGS GQWREAEWDE ALDYVAVSLK EVTEKYGNRA VAMTERANLN SHISKTFMKA
IGSPNYFTHD SCCKGSLNTA FRSLTGYADG SVSVDIPKTK HIILYGRNYF ESIELKAVKQ
LTGALDSGTR LTYIDPRITV TAAKSDDYLM IRPGTDLALN YALMHVIIKE GLYDAGYVDR
WVVGFDELQK FVVPYTPEWA EQETGIPARQ IISLARDAAA VKPAVIFHYG YRSSHYTNEV
YFRRSMIILN ALMGSIEAPG GIVFKKGAAE VGKKPLNKLT GQELPRVTEE RCDGVGTPRF
PTPDPAHGVV QLLPRVIMEQ DPYPVKALLV WRHDPVLSIP DYQYNKRAFS ELDFLVTIDI
NFSETAWLAD VILPESIYLE RGDSIQEING LKPSLFIRNA AVTPRHDTKP GWEIMKGIAD
RMGVGDYFPY NSLEELWAYQ LEGTGISLQD FEAKGFVTLA GEPIYWNRQN GIKFKTPSGK
IEFVSSLLEN NGIPSFPAYE PVRPPAEGSF RLMIGRNVAH THVSTQNNPL LNELLSENAL
WINGAQAEKL GIKNGGLVEV ESTRGKETLR ALVTDLIHPE AVFMLHGFGR RVPALTRCYN
KGGSDTALQE NITDMVGGSP ALQHVHVTVK PVVE
//
