ID   W9TFQ4_9PSED            Unreviewed;       258 AA.
AC   W9TFQ4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   Name=fpr_1 {ECO:0000313|EMBL:EXF47025.1};
GN   ORFNames=BAY1663_00523 {ECO:0000313|EMBL:EXF47025.1};
OS   Pseudomonas sp. BAY1663.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF47025.1, ECO:0000313|Proteomes:UP000019475};
RN   [1] {ECO:0000313|EMBL:EXF47025.1, ECO:0000313|Proteomes:UP000019475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAY1663 {ECO:0000313|EMBL:EXF47025.1,
RC   ECO:0000313|Proteomes:UP000019475};
RA   Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT   "Genome sequencing of Pseudomonas sp. BAY1663.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EXF47025.1}.
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DR   EMBL; AZSV01000004; EXF47025.1; -; Genomic_DNA.
DR   RefSeq; WP_037037691.1; NZ_AZSV01000004.1.
DR   AlphaFoldDB; W9TFQ4; -.
DR   STRING; 1439940.BAY1663_00523; -.
DR   PATRIC; fig|1439940.3.peg.529; -.
DR   eggNOG; COG1018; Bacteria.
DR   OrthoDB; 9784483at2; -.
DR   Proteomes; UP000019475; Unassembled WGS sequence.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   CDD; cd06195; FNR1; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR033892; FNR_bac.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR47878:SF1; FERREDOXIN--NADP(+) REDUCTASE; 1.
DR   PANTHER; PTHR47878; OXIDOREDUCTASE FAD/NAD(P)-BINDING DOMAIN PROTEIN; 1.
DR   Pfam; PF00970; FAD_binding_6; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PRINTS; PR00371; FPNCR.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019475}.
FT   DOMAIN          2..102
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   258 AA;  29445 MW;  174877FEC9FE25CB CRC64;
     MSNLNVERVL SVHHWNDTLF SFKTTRNPGL RFENGQFVMI GLEVEGRPLM RAYSIASPNY
     EEHLEFFSIK VPDGPLTSRL QHLQEGDQLM ISRKPTGTLV LDDLLPGKHL YLLSTGTGLA
     PFMSVIQDPE TYERFEKVVL VHGVRYVNEV AYREFITEHL PQNEFFGEAV KEKLIYYPTV
     TREPFEHQGR LTDLMRSGKL FSDIGLPPIN PQDDRAMICG SPSMLDETSQ VLDSFGLKVS
     PRMGDPGHYL IERAFVEK
//