ID   B8J1F9_DESDA            Unreviewed;       462 AA.
AC   B8J1F9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=BFD domain protein (2Fe-2S)-binding domain protein {ECO:0000313|EMBL:ACL49586.1};
GN   OrderedLocusNames=Ddes_1688 {ECO:0000313|EMBL:ACL49586.1};
OS   Desulfovibrio desulfuricans (strain ATCC 27774 / DSM 6949 / MB).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=525146 {ECO:0000313|EMBL:ACL49586.1};
RN   [1] {ECO:0000313|EMBL:ACL49586.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27774 {ECO:0000313|EMBL:ACL49586.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Sims D., Lu M., Kiss H., Meineke L., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Hazen T.C.;
RT   "Complete sequence of Desulfovibrio desulfuricans subsp. desulfuricans str.
RT   ATCC 27774.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001358; ACL49586.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8J1F9; -.
DR   STRING; 525146.Ddes_1688; -.
DR   KEGG; dds:Ddes_1688; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_030705_1_0_7; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd19946; GlpA-like_Fer2_BFD-like; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR007419; BFD-like_2Fe2S-bd_dom.
DR   InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR017224; Opine_Oxase_asu/HCN_bsu.
DR   PANTHER; PTHR42949; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   PANTHER; PTHR42949:SF2; ANAEROBIC GLYCEROL-3-PHOSPHATE DEHYDROGENASE SUBUNIT B; 1.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF037495; Opine_OX_OoxA/HcnB; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          6..316
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          374..425
FT                   /note="BFD-like [2Fe-2S]-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04324"
SQ   SEQUENCE   462 AA;  49215 MW;  9E70C4D006704CDE CRC64;
     MRSVWDVIIV GAGPAGMAAA IETASRGLLT LVLDRQSEAG GQIYKSIGSS ALSGKLGADY
     SAGLPLLQGF QNCGAVFTPC ANVWDVAADR VYVSVDGRSH CLLARQVVLA AGAMERPVPL
     PGWTLPGVIG SGASDILLKS ASLVPQGPVV LCGNGPLVLQ AAVHMHHFKV PVAGVLFTGR
     LGNMARAMRH AAWALARPGY FLHGMSMAAQ TFFKQKCLLG IRDISIIETG PEELAVNFTS
     LGGKKKRLAA ATVLLHEGVI SESRITRLAR CRHTWDQRQR YWHADADVWG QTSVPGLRTA
     GDVAGVRGAV AARAEGHLAG LDICRELGRL DMLRRDRHAA PHLRVLKRCR ALQPFLDEYF
     APTPAMLQPA DEAVVCRCEN LTGQTLRQAI SQGCYSPDGL KAQARPGMGP CQGRMCGQAV
     AEMIAHTQGL PLDALPQYTA QPPLFPLSLA QLADMTIPPD PS
//