ID   A0A0F2SEB1_9FIRM        Unreviewed;       938 AA.
AC   A0A0F2SEB1;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KJS49208.1};
GN   ORFNames=VR66_09730 {ECO:0000313|EMBL:KJS49208.1};
OS   Peptococcaceae bacterium BRH_c23.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae.
OX   NCBI_TaxID=1629714 {ECO:0000313|EMBL:KJS49208.1, ECO:0000313|Proteomes:UP000033503};
RN   [1] {ECO:0000313|EMBL:KJS49208.1, ECO:0000313|Proteomes:UP000033503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c23 {ECO:0000313|EMBL:KJS49208.1};
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:KJS49208.1}.
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DR   EMBL; LADV01000115; KJS49208.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2SEB1; -.
DR   PATRIC; fig|1629714.3.peg.412; -.
DR   Proteomes; UP000033503; 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:UniProtKB-KW.
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   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; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 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   Pfam; PF10518; TAT_signal; 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; PS51318; TAT; 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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          44..100
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   938 AA;  106032 MW;  5DF19B7541D199EC CRC64;
     MMNRRSFLKW TGAGAAAATL GTAGLFQLRP VKADELESLK NQGIDIKYTA DVMCPSECGL
     EMWVKDGRLT KIYGNKAVPF NDGTCCAKGA SGIQLVYSPD RIKYPMIREG ARGEGKFRKA
     TWDEAIDYIG KKLTKIKKEY GPESVIMDAG DVTDRDQYWR LFFAFGTPNV VEHGAICDTP
     RRHGPKLMFG GKRVEPDVMR PVFVRQPDGS LKKDMTYKNK LIIYVGWNPF VATRINYESR
     GTLAAKVDNG CKIVVVDPAL TNTGSQADLW LPIRPGTDGE LFAGMLRYIV ENDNPNSIDR
     RYIDWDFKKY SEGWDEYLEA FKSWWTKIDP MTNLPYFSLE WTAVRTGIEK EQIIELSHMF
     GSTKPAALVC GMQSPGHHYN GYVASILMTT LNVITGNFDV PGGVVDTEIT KSDKGGSATG
     KDFKKKKIKR TVNGVEVEGD VEQLHMDLFG DWPVAWDDVV GDFPKLFMEG VSLKYGAFKG
     HKYPIKAFLQ RTGNAVVTGS APYRWQEALT AKESSGEYKV ELMVTIDTIY LESALYADVI
     LPEASYAERM SLSDIYPPHP MIYLRDEVIK PLHESKPPTE IMNLIAKKLY ELGDKDIQPK
     DFWEKYKSQE DFVNEMLKPS PGKYNVGQPL PYPKLPEGYK LIGTPDSLED GRVTIDNEKK
     EIKGEAVTVE WLRKNKGVAV WPMSWYRYRK FDATSMEYVA NKAFPNTKTK LIEFKFNLYS
     AIDKKIQEGL DLPRGMKEIG WDRLPSTFYW FETTWNPHTN PKYKKYAEEY PFQIIVGRVH
     QTMSGTQMIP WLAQTPCEGI YMPLNNAFEH EILDANPEKK EGFELKAKKF KANTWCVGTT
     LMHSQDAAKL GLKSGDMIEI ENPLKRSVKS KVFVSEGIRP GVVKMGFGTG GRFSPGLGGT
     YKQKDYTPSH NMLVDPDSLS PLMGMPTYAD MVVKIKKL
//