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Database: UniProt
Entry: A0A0D3FPW5_9ORYZ
LinkDB: A0A0D3FPW5_9ORYZ
Original site: A0A0D3FPW5_9ORYZ 
ID   A0A0D3FPW5_9ORYZ        Unreviewed;       378 AA.
AC   A0A0D3FPW5;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Ferredoxin--NADP reductase, chloroplastic {ECO:0000256|PIRNR:PIRNR000361};
DE            Short=FNR {ECO:0000256|PIRNR:PIRNR000361};
DE            EC=1.18.1.2 {ECO:0000256|PIRNR:PIRNR000361};
OS   Oryza barthii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART03G36520.1};
RN   [1] {ECO:0000313|EnsemblPlants:OBART03G36520.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART03G36520.1};
RX   DOI=10.1007/s12284-009-9025-z;
RA   Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA   Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA   Knight J., Niazi F., Egholm M., Wing R.A.;
RT   "De novo next generation sequencing of plant genomes.";
RL   Rice 2:35-43(2009).
RN   [2] {ECO:0000313|EnsemblPlants:OBART03G36520.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
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;
CC         Evidence={ECO:0000256|ARBA:ARBA00001005,
CC         ECO:0000256|PIRNR:PIRNR000361};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- PATHWAY: Energy metabolism; photosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004748}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000256|PIRNR:PIRNR000361}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008312, ECO:0000256|PIRNR:PIRNR000361}.
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DR   AlphaFoldDB; A0A0D3FPW5; -.
DR   STRING; 65489.A0A0D3FPW5; -.
DR   PaxDb; 65489-OBART03G36520-1; -.
DR   EnsemblPlants; OBART03G36520.1; OBART03G36520.1; OBART03G36520.
DR   EnsemblPlants; OBART03G36540.1; OBART03G36540.1; OBART03G36540.
DR   Gramene; OBART03G36520.1; OBART03G36520.1; OBART03G36520.
DR   Gramene; OBART03G36540.1; OBART03G36540.1; OBART03G36540.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_053066_1_0_1; -.
DR   UniPathway; UPA00091; -.
DR   Proteomes; UP000026960; Chromosome 3.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniPathway.
DR   CDD; cd06208; CYPOR_like_FNR; 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; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR015701; FNR.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR035442; FNR_plant_Cyanobacteria.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43314; -; 1.
DR   PANTHER; PTHR43314:SF28; FERREDOXIN--NADP REDUCTASE, ROOT ISOZYME 2, CHLOROPLASTIC; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   PIRSF; PIRSF501178; FNR-PetH; 1.
DR   PIRSF; PIRSF000361; Frd-NADP+_RD; 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   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000361};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR000361};
KW   NADP {ECO:0000256|PIRNR:PIRNR000361, ECO:0000256|PIRSR:PIRSR000361-1};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000361};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960}.
FT   DOMAIN          93..221
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         156
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         176
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         237
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         299..300
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         309
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         337..338
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         376
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ   SEQUENCE   378 AA;  41848 MW;  7660E05E97221627 CRC64;
     MATAVASQVA VSAPAGSDRG LRSSGIQGSN NISFSNKSWV GTTLAWESKA ARPRHANKVL
     CMSVQQASES KVAVKPLDLE SANEPPLNTY KPKEPYTATI VSVERIVGPK APGETCHIVI
     DHGGNVPYWE GQSYGIIPPG ENPKKPGAPH NVRLYSIAST RYGDSFDGRT TSLCVRRAVY
     YDPETGKEDP SKNGVCSNFL CNSKPGDKVK VTGPSGKIML LPEEDPNATH IMIATGTGVA
     PFRGYLRRMF MEDVPKYRFG GLAWLFLGVA NTDSLLYDEE FTSYLKQYPD NFRYDKALSR
     EQKNKNAGKM YVQDKIEEYS DEIFKLLDGG AHIYFCGLKG MMPGIQDTLK KVAEQRGESW
     EQKLSQLKKN KQWHVEVY
//
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