FENR1_ORYSJ
ID FENR1_ORYSJ Reviewed; 362 AA.
AC P41344; Q0DF89; Q7F8E8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ferredoxin--NADP reductase, leaf isozyme 1, chloroplastic;
DE Short=FNR;
DE EC=1.18.1.2 {ECO:0000250|UniProtKB:Q9FKW6};
DE AltName: Full=Leaf FNR 1 {ECO:0000303|PubMed:26941088};
DE Short=FNR-1 {ECO:0000303|PubMed:26941088};
DE Short=Os-LFNR1 {ECO:0000303|PubMed:26941088};
DE Flags: Precursor;
GN Name=LFNR1 {ECO:0000303|PubMed:26941088};
GN OrderedLocusNames=Os06g0107700 {ECO:0000305}, LOC_Os06g01850 {ECO:0000305};
GN ORFNames=OsJ_19844 {ECO:0000312|EMBL:EAZ35558.1}, P0514G12.8, P0644B06.52;
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].
RC STRAIN=cv. Kinmaze; TISSUE=Leaf;
RX PubMed=8016278; DOI=10.1104/pp.104.4.1473;
RA Aoki H., Doyama N., Ida S.;
RT "Sequence of a cDNA encoding rice (Oryza sativa L.) leaf ferredoxin-NADP+
RT reductase.";
RL Plant Physiol. 104:1473-1474(1994).
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].
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 INTERACTION WITH LIR1 AND TIC62, AND DISULFIDE BOND.
RC STRAIN=cv. Nipponbare;
RX PubMed=26941088; DOI=10.1105/tpc.15.01027;
RA Yang C., Hu H., Ren H., Kong Y., Lin H., Guo J., Wang L., He Y., Ding X.,
RA Grabsztunowicz M., Mulo P., Chen T., Liu Y., Wu Z., Wu Y., Mao C., Wu P.,
RA Mo X.;
RT "LIGHT-INDUCED RICE1 regulates light-dependent attachment of LEAF-TYPE
RT FERREDOXIN-NADP+ OXIDOREDUCTASE to the thylakoid membrane in rice and
RT Arabidopsis.";
RL Plant Cell 28:712-728(2016).
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. {ECO:0000250|UniProtKB:Q9FKW6}.
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:0000250|UniProtKB:Q9FKW6};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- PATHWAY: Energy metabolism; photosynthesis.
CC {ECO:0000250|UniProtKB:Q9FKW6}.
CC -!- SUBUNIT: Component of high molecular weight thylakoid LFNRs-containing
CC protein complexes containing LIR1, LFNR1, LFNR2, TIC62 and TROL
CC proteins. Interacts directly with LIR1 and TIC62; LIR1 increases the
CC affinity of LFNR1 and LFNR2 for TIC62. {ECO:0000269|PubMed:26941088}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q9FKW6}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000250|UniProtKB:Q9FKW6}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9FKW6}; Stromal side
CC {ECO:0000250|UniProtKB:Q9FKW6}. Note=In the vicinity of the photosystem
CC I in the non-stacked and fringe portion of the membrane.
CC {ECO:0000250|UniProtKB:Q9FKW6}.
CC -!- PTM: May form interchain disulfide bonds with LIR1.
CC {ECO:0000269|PubMed:26941088}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D17790; BAA04616.1; -; mRNA.
DR EMBL; AP000616; BAA85425.1; -; Genomic_DNA.
DR EMBL; AP001129; BAA90642.1; -; Genomic_DNA.
DR EMBL; AP008212; BAF18484.1; -; Genomic_DNA.
DR EMBL; AP014962; BAS95764.1; -; Genomic_DNA.
DR EMBL; CM000143; EAZ35558.1; -; Genomic_DNA.
DR EMBL; AK065063; BAG89346.1; -; mRNA.
DR PIR; T04349; T04349.
DR RefSeq; XP_015640980.1; XM_015785494.1.
DR AlphaFoldDB; P41344; -.
DR SMR; P41344; -.
DR STRING; 4530.OS06T0107700-01; -.
DR PaxDb; P41344; -.
DR PRIDE; P41344; -.
DR EnsemblPlants; Os06t0107700-01; Os06t0107700-01; Os06g0107700.
DR GeneID; 4339874; -.
DR Gramene; Os06t0107700-01; Os06t0107700-01; Os06g0107700.
DR KEGG; osa:4339874; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_053066_0_0_1; -.
DR InParanoid; P41344; -.
DR OMA; DDYKATW; -.
DR OrthoDB; 817123at2759; -.
DR BRENDA; 1.18.1.2; 8948.
DR UniPathway; UPA00091; -.
DR Proteomes; UP000000763; Chromosome 6.
DR Proteomes; UP000007752; Chromosome 6.
DR Proteomes; UP000059680; Chromosome 6.
DR Genevisible; P41344; OS.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; IDA:UniProtKB.
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 Chloroplast; Disulfide bond; Electron transport; FAD; Flavoprotein;
KW Membrane; NADP; Oxidoreductase; Phosphoprotein; Photosynthesis; Plastid;
KW Reference proteome; Thylakoid; Transit peptide; Transport.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 63..362
FT /note="Ferredoxin--NADP reductase, leaf isozyme 1,
FT chloroplastic"
FT /id="PRO_0000019409"
FT DOMAIN 83..205
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 141..144
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 144
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 162..164
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 164
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 179..181
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00455"
FT BINDING 220
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 252..253
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 282..283
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 292
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 321..322
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 360
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT DISULFID 180..185
FT /evidence="ECO:0000250"
SQ SEQUENCE 362 AA; 40008 MW; 1B6034A8A76E4F29 CRC64;
MAAVTAAAVS TSAAAAVTKA SPSPAHCFLP CPPRTRAAHQ RGLLLRAQVS TTDAAAVAAA
PAKKEKISKK HDEGVVTNKY RPKEPYVGKC LLNTKITADD APGETWHMVF STEGEIPYRE
GQSIGVIADG VDKNGKPHKL RLYSIASSAL GDFGDSKTVS LCVKRLVYTN DQGEIVKGVC
SNFLCDLKPG SDVKITGPVG KEMLMPKDPN ANIIMLATGT GIAPFRSFLW KMFFEKYDDY
KFNGLAWLFL GVPTSSSLLY KEEFDKMKAK APENFRVDYA VSREQTNAQG EKMYIQTRMA
EYKEELWELL KKDHTYVYMC GLKGMEKGID DIMVSLAAKD GIDWADYKKQ LKKGEQWNVE
VY
