ID I4N8U1_9PSED Unreviewed; 259 AA.
AC I4N8U1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=PMM47T1_05194 {ECO:0000313|EMBL:EIK97881.1};
OS Pseudomonas sp. M47T1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1179778 {ECO:0000313|EMBL:EIK97881.1, ECO:0000313|Proteomes:UP000004339};
RN [1] {ECO:0000313|EMBL:EIK97881.1, ECO:0000313|Proteomes:UP000004339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M47T1 {ECO:0000313|EMBL:EIK97881.1,
RC ECO:0000313|Proteomes:UP000004339};
RX PubMed=22887683; DOI=10.1128/JB.01116-12;
RA Proenca D.N., Espirito Santo C., Grass G., Morais P.V.;
RT "Draft Genome Sequence of Pseudomonas sp. Strain M47T1, Carried by
RT Bursaphelenchus xylophilus Isolated from Pinus pinaster.";
RL J. Bacteriol. 194:4789-4790(2012).
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:EIK97881.1}.
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DR EMBL; AJWX01000003; EIK97881.1; -; Genomic_DNA.
DR RefSeq; WP_002554680.1; NZ_AJWX01000003.1.
DR AlphaFoldDB; I4N8U1; -.
DR STRING; 1179778.PMM47T1_05194; -.
DR GeneID; 77277343; -.
DR PATRIC; fig|1179778.3.peg.1039; -.
DR eggNOG; COG1018; Bacteria.
DR OrthoDB; 9784483at2; -.
DR Proteomes; UP000004339; 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:UP000004339}.
FT DOMAIN 2..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 259 AA; 29667 MW; EFC13B8F84C53CA4 CRC64;
MSNMNHERVL SVHHWNDTLF SFKCTRDPGL RFENGQFVMI GLQQPNGRPL MRAYSIASPN
WEEHLEFFSI KVPDGPLTSQ LQHLKEGDEI IISKKPTGTL VLDDLKPGKH LYLLSTGTGL
APFMSVIQDP ETYERFEKVI LCHGVRYVNE VAYREFITEH LPQNEFFGEA LRDKLIYYPT
VTREPFENEG RLTDLMRSGK LFSDIGLPPI NPQDDRAMLC GSPSMLDETS EVLNSFGLTV
SPRMREPGDY LIERAFVEK
//
