FENR2_ORYSI
ID FENR2_ORYSI Reviewed; 366 AA.
AC A2WZT1;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ferredoxin--NADP reductase, leaf isozyme 2, chloroplastic;
DE EC=1.18.1.2 {ECO:0000250|UniProtKB:Q9FKW6};
DE AltName: Full=Leaf FNR 2 {ECO:0000305};
DE Short=FNR-2 {ECO:0000305};
DE Short=Os-LFNR2 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=OsI_05475 {ECO:0000312|EMBL:EAY84091.1};
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 LFNR1 (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:Q6ZFJ3,
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:Q6ZFJ3}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; CM000127; EAY84091.1; -; Genomic_DNA.
DR AlphaFoldDB; A2WZT1; -.
DR SMR; A2WZT1; -.
DR STRING; 39946.A2WZT1; -.
DR PRIDE; A2WZT1; -.
DR EnsemblPlants; BGIOSGA007302-TA; BGIOSGA007302-PA; BGIOSGA007302.
DR Gramene; BGIOSGA007302-TA; BGIOSGA007302-PA; BGIOSGA007302.
DR HOGENOM; CLU_053066_0_0_1; -.
DR OMA; CYREACV; -.
DR UniPathway; UPA00091; -.
DR Proteomes; UP000007015; Chromosome 2.
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..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..366
FT /note="Ferredoxin--NADP reductase, leaf isozyme 2,
FT chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000442380"
FT DOMAIN 87..209
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 145..148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 148
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 166..168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 168
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 172
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 183..185
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 224
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P00455"
FT BINDING 224
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 256..257
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 286..287
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 296
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 325..326
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT BINDING 364
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P10933"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9FKW6"
FT DISULFID 184..189
FT /evidence="ECO:0000250"
SQ SEQUENCE 366 AA; 40693 MW; 08C577FDDEE6E0EA CRC64;
MAAVNTVSSL PCSKAGAAVA GGAPRPSTCS VFYPPRCWSK RSSGNGVRAQ ASTTETTAAP
AAEVTTKVEK VSKKQVDGVV TNKYRPKEPY TGRCLLNTRI TGDDAPGETW HMVFSTDGEI
PYREGQSIGV IPDGIDKNGK PHKLRLYSIA SSAIGDFADS KTVSLCVKRL VYTNDKGEIV
KGVCSNFLCD LKPGSDVKIT GPVGKEMLMP KDPNATIIML GTGTGIAPFR SFLWKMFFEE
HDDYRFNGLA WLFLGVPTSS TLLYREEFER MKEIAPERFR LDFAVSREQT NAAGEKMYIQ
TRMAEYKDEL WELLKKDNTY VYMCGLKGME KGIDDIMIDL AAKDGIDWLD YKKQLKKSEQ
WNVEVY
