FENR3_ORYSJ
ID FENR3_ORYSJ Reviewed; 378 AA.
AC O23877; A0A0P0X2G7; Q0D8L9; Q6ZF67;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ferredoxin--NADP reductase, embryo isozyme, chloroplastic;
DE Short=FNR;
DE EC=1.18.1.2;
DE Flags: Precursor;
GN OrderedLocusNames=Os07g0147900 {ECO:0000312|EMBL:BAF20804.1},
GN LOC_Os07g05400 {ECO:0000305};
GN ORFNames=OsJ_23093 {ECO:0000312|EMBL:EAZ38695.1}, P0022E03.21-1;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Nipponbare;
RA Aoki H., Kumada H.O., Masumura T., Tanaka K., Ida S.;
RT "Cloning and nucleotide sequence of a cDNA encoding rice embryo ferredoxin-
RT NADP+ oxidoreductase.";
RL (er) Plant Gene Register PGR96-115(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [7]
RP PROTEIN SEQUENCE OF 281-289.
RC STRAIN=cv. Nipponbare; TISSUE=Stem;
RX PubMed=14681440; DOI=10.1093/nar/gkh020;
RA Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT "Rice proteome database based on two-dimensional polyacrylamide gel
RT electrophoresis: its status in 2003.";
RL Nucleic Acids Res. 32:D388-D392(2004).
CC -!- FUNCTION: May play a key role in regulating the relative amounts of
CC cyclic and non-cyclic electron flow to meet the demands of the plant
CC for ATP and reducing power. Is involved in nitrate assimilation.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Energy metabolism; photosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O23877-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O23877-2; Sequence=VSP_017442;
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; D87547; BAA13417.1; -; mRNA.
DR EMBL; AP004263; BAC83340.1; -; Genomic_DNA.
DR EMBL; AP008213; BAF20804.1; -; Genomic_DNA.
DR EMBL; AP014963; BAT00063.1; -; Genomic_DNA.
DR EMBL; CM000144; EAZ38695.1; -; Genomic_DNA.
DR EMBL; AK072768; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T02977; T02977.
DR RefSeq; XP_015646844.1; XM_015791358.1. [O23877-1]
DR AlphaFoldDB; O23877; -.
DR SMR; O23877; -.
DR STRING; 4530.OS07T0147900-01; -.
DR PaxDb; O23877; -.
DR PRIDE; O23877; -.
DR EnsemblPlants; Os07t0147900-01; Os07t0147900-01; Os07g0147900. [O23877-1]
DR GeneID; 4342399; -.
DR Gramene; Os07t0147900-01; Os07t0147900-01; Os07g0147900. [O23877-1]
DR KEGG; osa:4342399; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_053066_1_0_1; -.
DR InParanoid; O23877; -.
DR OMA; WLFMGVA; -.
DR OrthoDB; 817123at2759; -.
DR UniPathway; UPA00091; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000007752; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; O23877; baseline and differential.
DR Genevisible; O23877; OS.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR GO; GO:0031984; C:organelle subcompartment; IEA:UniProt.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.80; -; 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; PTHR43314; 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; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Direct protein sequencing;
KW Electron transport; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Photosynthesis; Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT CHAIN 63..378
FT /note="Ferredoxin--NADP reductase, embryo isozyme,
FT chloroplastic"
FT /id="PRO_0000019417"
FT DOMAIN 93..221
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 153..156
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 174..176
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 195..197
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 269..270
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 299..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 337..338
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..218
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_017442"
SQ SEQUENCE 378 AA; 41815 MW; CDDB2CFBC4689145 CRC64;
MASALGAQAS VAAPIGAGGY GRSSSSKGSN TVNFCNKSWI GTTLAWESKA LKSRHMNKIF
SMSVQQASKS KVAVKPLELD NAKEPPLNLY KPKEPYTATI VSVERLVGPK APGETCHIVI
DHGGNVPYWE GQSYGVIPPG ENPKKPGSPN TVRLYSIAST RYGDSFDGKT ASLCVRRAVY
YDPETGKEDP TKKGICSNFL CDSKPGDKVQ ITGPSGKIML LPEDDPNATH IMIATGTGVA
PYRGYLRRMF MEDVPSFKFG GLAWLFLGVA NTDSLLYDEE FTNYLQQYPD NFRYDKALSR
EQKNKNGGKM YVQDKIEEYS DEIFKLLDGG AHIYFCGLKG MMPGIQDTLK RVAEQRGESW
EQKLSQLKKN KQWHVEVY
