FENR2_TOBAC
ID FENR2_TOBAC Reviewed; 375 AA.
AC O04397;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ferredoxin--NADP reductase, root-type isozyme, chloroplastic;
DE Short=FNR;
DE EC=1.18.1.2;
DE Flags: Precursor;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Bright Yellow 2;
RA Kumada H.O., Aoki H., Doyama N., Ida S.;
RT "Nucleotide sequence of a ferredoxin-NADP+ oxidoreductase cDNA from
RT cultured tobacco cells.";
RL (er) Plant Gene Register PGR98-038(1998).
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 -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AB004307; BAA20365.1; -; mRNA.
DR PIR; T02215; T02215.
DR RefSeq; NP_001313084.1; NM_001326155.1.
DR AlphaFoldDB; O04397; -.
DR SMR; O04397; -.
DR STRING; 4097.O04397; -.
DR GeneID; 107825625; -.
DR KEGG; nta:107825625; -.
DR UniPathway; UPA00091; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Chloroplast; Electron transport; FAD; Flavoprotein; NADP; Oxidoreductase;
KW Photosynthesis; Plastid; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..375
FT /note="Ferredoxin--NADP reductase, root-type isozyme,
FT chloroplastic"
FT /id="PRO_0000019416"
FT DOMAIN 91..219
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 151..154
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 172..174
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 193..195
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 266..267
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 296..297
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 306
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 334..335
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 375 AA; 41958 MW; AB5ED3988F746B92 CRC64;
MAHSALSQVS VAVPLQTDSS FRRSTFKATS ITFSDRSSWI SMPPIDLKAA PSRNQHIVCM
SVQQASKAKV SVSPLSLEDA KEPPLNIYKP KEPYTATIVS VERLVGPKAP GETCHIVIDH
DGNLPYWEGQ SYGVIPPGEN PKKPGNPHNV RLYLIASTRY GDSFDGKTAS LCVRRAVYYD
PETGKEDPSK NGVCSNFLCD SKPGDKVKIT GPSGKIMLLP EEIPNATHIM IGTGTGVAPF
RGYLRRMFME SVPTKFNGLA WLFLGVANTD SLLYDDEFTK YLNDYPGNFR YDRALSREQK
NNKGGKMYVQ DKIEEYSDEI FKLLDEGAHI YFCGLKGMMP GIQDTLKRVA ERRGESWEQK
LSQLKKNKQW HVEVY
