ID A0A1R1QSG2_9BACI Unreviewed; 349 AA.
AC A0A1R1QSG2; A0A1R1RMZ1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 ORFNames=BTA30_18150 {ECO:0000313|EMBL:OMI27368.1}, BW143_06735
GN {ECO:0000313|EMBL:OMI07578.1};
OS Bacillus swezeyi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1925020 {ECO:0000313|EMBL:OMI07578.1, ECO:0000313|Proteomes:UP000187367};
RN [1] {ECO:0000313|EMBL:OMI07578.1, ECO:0000313|Proteomes:UP000187367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41282 {ECO:0000313|EMBL:OMI07578.1,
RC ECO:0000313|Proteomes:UP000187367}, and NRRL B-41294
RC {ECO:0000313|EMBL:OMI27368.1, ECO:0000313|Proteomes:UP000187536};
RA Dunlap C.;
RT "Bacillus phylogenomics.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OMI07578.1}.
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DR EMBL; MTJL01000010; OMI07578.1; -; Genomic_DNA.
DR EMBL; MRBK01000025; OMI27368.1; -; Genomic_DNA.
DR RefSeq; WP_076762709.1; NZ_MTJL01000010.1.
DR AlphaFoldDB; A0A1R1QSG2; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000187367; Unassembled WGS sequence.
DR Proteomes; UP000187536; Unassembled WGS sequence.
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..308
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; 38292 MW; 152181CE49432273 CRC64;
MSRNEVFDVT VIGGGPAGLY SAFYSGLRGM KTKIIEYQPM LGGKVHVYPE KMIWDIGGQT
PIPGAKLIEQ MVQQGLTFHP EVLLNEKVDS IARNEEGLFE LHTAATGVHL SKTVIVAVGG
GILNPQKLQI EGAERFEVSN LNYTVKSLQH FKDKAVIVSG GGNSAVDWAN ELEPVAKKVY
LAYRKEALSG HEAQVDQLLN SSVSCFFHTE ITKLIASDDH EAIERVELTN AQTGEVTVLP
VDEVIINHGY ERDKSLLENS RLDITRVDDY FIAGTANCQS SVPGLYAAGD ILHYEGKLHL
IAGAFQDAAN AVNSAKRFID PEAHKSAMVS SHNEVFKERN RELVKKMFG
//
