ID   A0A0H3KHE2_BURM1        Unreviewed;       411 AA.
AC   A0A0H3KHE2;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Ferredoxin-NAD+ reductase {ECO:0000313|EMBL:BAG44533.1};
DE            EC=1.18.1.3 {ECO:0000313|EMBL:BAG44533.1};
GN   Name=hcaD {ECO:0000313|EMBL:BAG44533.1};
GN   OrderedLocusNames=BMULJ_02643 {ECO:0000313|EMBL:BAG44533.1};
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019 {ECO:0000313|EMBL:BAG44533.1, ECO:0000313|Proteomes:UP000008815};
RN   [1] {ECO:0000313|EMBL:BAG44533.1, ECO:0000313|Proteomes:UP000008815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249 {ECO:0000313|Proteomes:UP000008815};
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP009385; BAG44533.1; -; Genomic_DNA.
DR   RefSeq; WP_012212758.1; NC_010804.1.
DR   AlphaFoldDB; A0A0H3KHE2; -.
DR   STRING; 395019.BMULJ_02643; -.
DR   KEGG; bmj:BMULJ_02643; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_4_0_4; -.
DR   Proteomes; UP000008815; Chromosome 1.
DR   GO; GO:0008860; F:ferredoxin-NAD+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
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; 1.
DR   SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:BAG44533.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008815}.
FT   DOMAIN          8..303
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          322..410
FT                   /note="Reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14759"
SQ   SEQUENCE   411 AA;  43885 MW;  78B8725C20012549 CRC64;
     MTNDRVMAIV GAGHAGGRAA QVLREYGWRG RIVLIGAEPH LPYERPPLSK GVLTGERSAA
     QCALRDRDAW RADAIEPIVA TVERIDPAAR EIRVSDGRAF AYDALLLATG GRARRLAIPG
     ADLDGVLALR TLDDAAALGA RLVRDARIVL IGGGFIGLEV AASARRRGCR VTVLDAASRV
     LGRAVPDTIA ARVHALHVRH GVAIRLNRAP VAIERTAGGA LAVVLDDGDT LIADTVVVGI
     GIEPADELAR DAGLAVDRGI VVDERLETSA RGIYAAGDVA VFPGGSSARR VRQETWHGAE
     TQARVAARNM LGADEPYRDV RWFWSDQYDA QLQVVGEPAL GERTVARVLD DDAEIRFHFD
     AQARLVAASG FGCAPTWVKE MRVARMLVER AADVTPADVA DTGVKLKSLL R
//