ID A0A0Q9XII2_9STAP Unreviewed; 343 AA.
AC A0A0Q9XII2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ACA31_10585 {ECO:0000313|EMBL:KRG08208.1};
OS Staphylococcus sp. NAM3COL9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1667172 {ECO:0000313|EMBL:KRG08208.1, ECO:0000313|Proteomes:UP000051126};
RN [1] {ECO:0000313|EMBL:KRG08208.1, ECO:0000313|Proteomes:UP000051126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA309 {ECO:0000313|EMBL:KRG08208.1,
RC ECO:0000313|Proteomes:UP000051126};
RA Gaiero J., Nicol R., Habash M.;
RT "Genome sequencing project of Staphylococcus sp. NA309.";
RL Submitted (JUN-2015) 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:KRG08208.1}.
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DR EMBL; LGPC01000016; KRG08208.1; -; Genomic_DNA.
DR RefSeq; WP_057513280.1; NZ_LGPC01000016.1.
DR AlphaFoldDB; A0A0Q9XII2; -.
DR PATRIC; fig|1667172.3.peg.2142; -.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000051126; 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|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01685};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01685}; NADP {ECO:0000256|HAMAP-Rule:MF_01685};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01685}.
FT DOMAIN 3..290
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 31
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 83
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 118
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 285
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 326
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
SQ SEQUENCE 343 AA; 37954 MW; EC9022468209C8D8 CRC64;
MDDVIIIGGG PAGLYASFYA GLRGMSVRII DIQDKLGGKM HVYPEKIIWD IGGLAPKPCA
EVIKDTVAQG LHFNPEVNLE ERVIDIRKIA EQHFEIETDK HNIYDAKSVI IAIGGGIINP
KQLDIKDAER YKLTNLNYVV QSLKKFKDKN VLISGAGNSA LDWANDLSGY AKSITLIYRK
ADIKGYEAMK GVLDKLEVEK LSNTHIHQLI GDSTQTKIEQ VILENTETKE QIAKIFDEVI
ISHGFDHEST LLEESSTQVD MFNEYSIKGF GNTSTSIEGL YACGDVIYHE AKAHLIASAF
SDAANAANLA KLYVEPEASP EGYVSSHNDV FKESNKVVMK KYL
//
