ID J2ZI05_9PSED Unreviewed; 259 AA.
AC J2ZI05;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=PMI28_04527 {ECO:0000313|EMBL:EJM52593.1};
OS Pseudomonas sp. GM48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144330 {ECO:0000313|EMBL:EJM52593.1, ECO:0000313|Proteomes:UP000007293};
RN [1] {ECO:0000313|EMBL:EJM52593.1, ECO:0000313|Proteomes:UP000007293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM48 {ECO:0000313|EMBL:EJM52593.1,
RC ECO:0000313|Proteomes:UP000007293};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(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:EJM52593.1}.
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DR EMBL; AKJM01000121; EJM52593.1; -; Genomic_DNA.
DR RefSeq; WP_003443014.1; NZ_AKJM01000121.1.
DR AlphaFoldDB; J2ZI05; -.
DR GeneID; 66647568; -.
DR PATRIC; fig|1144330.3.peg.4415; -.
DR OrthoDB; 9784483at2; -.
DR Proteomes; UP000007293; 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}.
FT DOMAIN 2..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 259 AA; 29694 MW; EFC13B8F92A9ECA4 CRC64;
MSNMNHERVL SVHHWNDTLF SFKCTRDPGL RFENGQFVMI GLQQPNGRPL MRAYSIASPN
WEEHLEFFSI KVPDGPLTSQ LQHLKEGDEI IISKKPTGTL VLDDLKPGKH LYLLSTGTGL
APFMSVIQDP ETYERFEKVI LCHGVRYVNE VAYREFITEH LPQNEFFGEA LRDKLIYYPT
VTREPFENEG RLTDLMRSGK LFSDIGLPPI NPQDDRAMLC GSPSMLDETS EVLNSFGLKV
SPRMREPGDY LIERAFVEK
//
