FENR1_ORYSI
ID FENR1_ORYSI Reviewed; 362 AA.
AC A2Y8E0;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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:0000305};
DE Short=FNR-1 {ECO:0000305};
DE Short=Os-LFNR1 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=OsI_21320 {ECO:0000312|EMBL:EAY99350.1};
OS Oryza sativa subsp. indica (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=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
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).
CC -!- FUNCTION: Plays a key role in regulating the relative amounts of cyclic
CC and non-cyclic electron flow to meet the demands of the plant for ATP
CC 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 Evidence={ECO:0000250|UniProtKB:Q9FKW6};
CC -!- PATHWAY: Energy metabolism; photosynthesis.
CC {ECO:0000250|UniProtKB:Q9FKW6}.
CC -!- SUBUNIT: Heterodimer with LFNR2 (By similarity). Component of high
CC molecular weight thylakoid LFNRs-containing protein complexes
CC containing LIR1, LFNR1, LFNR2, TIC62 and TROL proteins. Interacts
CC directly with LFNR1 and LFNR2; LIR1 increases the affinity of LFNR1 and
CC LFNR2 for TIC62 and subsequent thylakoid relocalization (By
CC similarity). {ECO:0000250|UniProtKB:P41344,
CC ECO:0000250|UniProtKB:Q9FKW6}.
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}.
CC -!- PTM: May form interchain disulfide bonds with LIR1.
CC {ECO:0000250|UniProtKB:P41344}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; CM000131; EAY99350.1; -; Genomic_DNA.
DR AlphaFoldDB; A2Y8E0; -.
DR SMR; A2Y8E0; -.
DR STRING; 39946.A2Y8E0; -.
DR PRIDE; A2Y8E0; -.
DR EnsemblPlants; BGIOSGA022091-TA; BGIOSGA022091-PA; BGIOSGA022091.
DR Gramene; BGIOSGA022091-TA; BGIOSGA022091-PA; BGIOSGA022091.
DR HOGENOM; CLU_053066_0_0_1; -.
DR OMA; CVKRHRY; -.
DR UniPathway; UPA00091; -.
DR Proteomes; UP000007015; Chromosome 6.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; ISS: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 3: Inferred from homology;
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..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..362
FT /note="Ferredoxin--NADP reductase, leaf isozyme 1,
FT chloroplastic"
FT /id="PRO_0000442378"
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; 39985 MW; 1FF6EFC1876E4F29 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 KKDNTYVYMC GLKGMEKGID DIMVSLAAKD GIDWADYKKQ LKKGEQWNVE
VY
