ID   A0A2X4X8G3_9NOCA        Unreviewed;       408 AA.
AC   A0A2X4X8G3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Ferredoxin reductase {ECO:0000313|EMBL:SQI32844.1};
DE            EC=1.18.1.- {ECO:0000313|EMBL:SQI32844.1};
GN   Name=thcD_1 {ECO:0000313|EMBL:SQI32844.1};
GN   ORFNames=NCTC10994_02339 {ECO:0000313|EMBL:SQI32844.1};
OS   Rhodococcus coprophilus.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=38310 {ECO:0000313|EMBL:SQI32844.1, ECO:0000313|Proteomes:UP000249091};
RN   [1] {ECO:0000313|EMBL:SQI32844.1, ECO:0000313|Proteomes:UP000249091}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10994 {ECO:0000313|EMBL:SQI32844.1,
RC   ECO:0000313|Proteomes:UP000249091};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; LS483468; SQI32844.1; -; Genomic_DNA.
DR   RefSeq; WP_072704974.1; NZ_LS483468.1.
DR   AlphaFoldDB; A0A2X4X8G3; -.
DR   STRING; 1219011.GCA_001895045_04116; -.
DR   KEGG; rcr:NCTC10994_02339; -.
DR   Proteomes; UP000249091; Chromosome 1.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR028202; Reductase_C.
DR   PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR   PANTHER; PTHR43557:SF2; RIESKE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF14759; Reductase_C; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:SQI32844.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249091}.
FT   DOMAIN          5..296
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          320..401
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   408 AA;  43611 MW;  D9E387E2C17C6E9C CRC64;
     MTLRTVVTVG AGQVAAGAAR TLRRRGFDGR IILLGDESHA PYQRPPLSKE FLAGRESAES
     LSLFTPRWLE ANDIEIRTGV TVRRIDTTTG SVEFDGGSVA ADAVVLATGG RPRTIESTGP
     RPDLVHYLRT LDDALALAPR LIPGSRLIVV GGGFIGLEIA ATARSLGVEV TVVEQSAHLL
     GSVLGPQVGN YCADLHRRNG INLHTGTGVV TVTTSDRGVR IITTTGDTIE ADAAVVGIGI
     VPDTQVAAAS GLSVDNGIVV DEHGRTSIPN IYAAGDVANR FSPRAGRHIR VEHFDNANRQ
     STVVADTIVG RTKLSDDPHW FWSDQYDTNI QFAGTPLGTT DFVIRGDIET GEFSVFYLAG
     DTLTAAFAMD RGEDIMAARE LLGRQVDPAR LADEDTDLWE MYEEVEPA
//