ID B9J2H7_BACCQ Unreviewed; 349 AA.
AC B9J2H7;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Ferredoxin--NADP reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE Short=FNR {ECO:0000256|HAMAP-Rule:MF_01685};
DE Short=Fd-NADP(+) reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE EC=1.18.1.2 {ECO:0000256|HAMAP-Rule:MF_01685};
GN Name=trxB {ECO:0000313|EMBL:ACM10896.1};
GN OrderedLocusNames=BCQ_0424 {ECO:0000313|EMBL:ACM10896.1};
OS Bacillus cereus (strain Q1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100 {ECO:0000313|EMBL:ACM10896.1, ECO:0000313|Proteomes:UP000000441};
RN [1] {ECO:0000313|EMBL:ACM10896.1, ECO:0000313|Proteomes:UP000000441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1 {ECO:0000313|EMBL:ACM10896.1,
RC ECO:0000313|Proteomes:UP000000441};
RX PubMed=19060151; DOI=10.1128/JB.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2
CC oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:20125, Rhea:RHEA-
CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.18.1.2; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01685};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01685};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01685};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01685}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC {ECO:0000256|HAMAP-Rule:MF_01685}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01685}.
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DR EMBL; CP000227; ACM10896.1; -; Genomic_DNA.
DR AlphaFoldDB; B9J2H7; -.
DR KEGG; bcq:BCQ_0424; -.
DR HOGENOM; CLU_031864_5_5_9; -.
DR Proteomes; UP000000441; Chromosome.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR HAMAP; MF_01685; FENR2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR022890; Fd--NADP_Rdtase_type_2.
DR PANTHER; PTHR48105:SF18; FERREDOXIN--NADP REDUCTASE; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_01685};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01685};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01685};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01685}.
FT DOMAIN 7..306
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 123
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 290
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 331
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
SQ SEQUENCE 349 AA; 38671 MW; 33A889DCF69A916E CRC64;
MNREELFDVT VIGGGPAGLY SAFYSGLREM KTKIIEFQPQ LGGKIHVYPE KMIWDVGGLL
PVTGDKLIEQ LVQQGLTFQP EVVLNTKVES IIRNKDGTFT LKANDGKEHF SKTVIVATGS
GILKPQKLSI EGAERFEVSN LNYTVKSLKR FKDKTIIISG GGNSAVDWAN ELEPIAKKVY
VTYRKEELSG HEAQVKQLLN SSAECFFHTS ITKLIAGDSH EAIEYVELTN HETGEVSHLP
IDEVIINHGY ERDITLLENS ELDVAIIDNF YIAGNANSES SVDGLYAAGD ILKHEGKLHL
IAGAFQDAGN AVNKAKQFIQ PDASEYGMVS SHNEVFKKRN RELIKQMMK
//
