ID B0KT29_PSEPG Unreviewed; 259 AA.
AC B0KT29;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN OrderedLocusNames=PputGB1_1240 {ECO:0000313|EMBL:ABY97147.1};
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869 {ECO:0000313|EMBL:ABY97147.1, ECO:0000313|Proteomes:UP000002157};
RN [1] {ECO:0000313|EMBL:ABY97147.1, ECO:0000313|Proteomes:UP000002157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1 {ECO:0000313|EMBL:ABY97147.1,
RC ECO:0000313|Proteomes:UP000002157};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP000926; ABY97147.1; -; Genomic_DNA.
DR RefSeq; WP_012270923.1; NC_010322.1.
DR AlphaFoldDB; B0KT29; -.
DR KEGG; ppg:PputGB1_1240; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_3_0_6; -.
DR Proteomes; UP000002157; Chromosome.
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}.
FT DOMAIN 2..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 259 AA; 29671 MW; 76F7106CA6237E04 CRC64;
MSNMNHERVL SVHHWNDTLF SFKCTRDPGL RFENGQFVMI GLQQESGRPL MRAYSIASPN
WEEHLEFFSI KVPDGPLTSQ LQHLKEGDEI IISKKPTGTL VLDDLNPGKH LYLLSTGTGL
APFMSVIQDP ETYERFEKVI LVHGVRYVNE VAYREFITEH LPQNEFFGES VREKLIYYPT
VTREPFENQG RLTDLMRSGK LFSDIGLPPI NPQDDRAMIC GSPSMLDETS EVLDSFGLKV
SARMREPGDY LIERAFVEK
//
