ID A0A0A5HVC9_9BACI Unreviewed; 349 AA.
AC A0A0A5HVC9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=N784_15150 {ECO:0000313|EMBL:KGX87582.1};
OS Pontibacillus litoralis JSM 072002.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX87582.1, ECO:0000313|Proteomes:UP000030401};
RN [1] {ECO:0000313|EMBL:KGX87582.1, ECO:0000313|Proteomes:UP000030401}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX87582.1,
RC ECO:0000313|Proteomes:UP000030401};
RA Huang J., Wang G.;
RL Submitted (AUG-2013) 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|HAMAP-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:KGX87582.1}.
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DR EMBL; AVPG01000006; KGX87582.1; -; Genomic_DNA.
DR RefSeq; WP_036833369.1; NZ_AVPG01000006.1.
DR AlphaFoldDB; A0A0A5HVC9; -.
DR STRING; 1385512.N784_15150; -.
DR eggNOG; COG0492; Bacteria.
DR OrthoDB; 9806179at2; -.
DR Proteomes; UP000030401; 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; 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; PF03486; HI0933_like; 1.
DR Pfam; PF13738; Pyr_redox_3; 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}; Reference proteome {ECO:0000313|Proteomes:UP000030401}.
FT BINDING 35
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 47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 122
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
SQ SEQUENCE 349 AA; 38632 MW; 8A5F25844FD13339 CRC64;
MKHECFDVTI IGGGPAGLFS AFYSGLREMK TKIIEYQPKL GGKIHVYPEK MIWDIGGLPP
LTGQQLIHQL TEQAMTFQPK IVLNEKVESI SKLENDSFVL TGSSGEKHYS KTVIVAVGGG
ILNPQKLNIE GAERFEISNL QYTIKSLGRF KGKTVIISGG GNSAIDWANE LEPIAKQVYV
TYRKDQLKGH EAQVSQLLNS SAKCFFHTSI TKLIASEDQD VIEKVELTNY NTGETFTLAI
DDVIINHGFD RDKSLLDNSD IEVDRVRDYF IDGNSLSESS VEGLYAAGDI LAHEGKLHLI
AGAFQDAANA VNRAKQYIDP EANASGMVSS HNDIFKKRNK QFIKQMMKL
//
