FENR1_PEA
ID FENR1_PEA Reviewed; 360 AA.
AC P10933;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ferredoxin--NADP reductase, leaf isozyme, chloroplastic;
DE Short=FNR;
DE EC=1.18.1.2;
DE Flags: Precursor;
GN Name=PETH;
OS Pisum sativum (Garden pea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX NCBI_TaxID=3888;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Little Marvel; TISSUE=Leaf;
RX AGRICOLA=IND92000035; DOI=10.1007/BF00033606;
RA Newman B.J., Gray J.C.;
RT "Characterisation of a full-length cDNA clone for pea ferredoxin-NADP+
RT reductase.";
RL Plant Mol. Biol. 10:511-520(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 270-360, AND MUTAGENESIS OF TYR-360.
RX PubMed=8366077; DOI=10.1016/s0021-9258(19)36509-3;
RA Orellano E.G., Calcaterra N.B., Carrillo N., Ceccarelli E.A.;
RT "Probing the role of the carboxyl-terminal region of ferredoxin-NADP+
RT reductase by site-directed mutagenesis and deletion analysis.";
RL J. Biol. Chem. 268:19267-19273(1993).
RN [3]
RP INTERACTION WITH TIC62.
RX PubMed=12426385; DOI=10.1093/emboj/cdf621;
RA Kuechler M., Decker S., Hoermann F., Soll J., Heins L.;
RT "Protein import into chloroplasts involves redox-regulated proteins.";
RL EMBO J. 21:6136-6145(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH FAD AND NADP.
RX PubMed=10467097; DOI=10.1038/12307;
RA Deng Z., Aliverti A., Zanetti G., Arakaki A.K., Ottado J., Orellano E.G.,
RA Calcaterra N.B., Ceccarelli E.A., Carrillo N., Karplus P.A.;
RT "A productive NADP+ binding mode of ferredoxin-NADP + reductase revealed by
RT protein engineering and crystallographic studies.";
RL Nat. Struct. Biol. 6:847-853(1999).
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.
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 -!- SUBUNIT: Monomer. Interacts with TIC62 (via C-terminus).
CC {ECO:0000269|PubMed:10467097, ECO:0000269|PubMed:12426385}.
CC -!- INTERACTION:
CC P10933; P09911: PETF; NbExp=3; IntAct=EBI-931306, EBI-931449;
CC P10933; Q8SKU2: TIC62; NbExp=5; IntAct=EBI-931306, EBI-15606082;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma. Plastid, chloroplast
CC thylakoid membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Stromal side {ECO:0000305}. Note=In the vicinity of the
CC photosystem I in the non-stacked and fringe portion of the membrane.
CC -!- MISCELLANEOUS: FNR is probably attached to the membrane by a specific
CC binding protein.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X12446; CAA30978.1; -; mRNA.
DR EMBL; L15565; AAB59349.1; -; mRNA.
DR EMBL; L15567; AAB59303.1; -; mRNA.
DR EMBL; L15569; AAB59304.1; -; mRNA.
DR PIR; S04030; S04030.
DR PDB; 1QFY; X-ray; 1.80 A; A/B=53-360.
DR PDB; 1QFZ; X-ray; 1.70 A; A/B=53-360.
DR PDB; 1QG0; X-ray; 2.50 A; A/B=53-360.
DR PDB; 1QGA; X-ray; 2.00 A; A/B=53-360.
DR PDB; 2XNC; X-ray; 2.90 A; A/B=53-360.
DR PDB; 3MHP; X-ray; 1.70 A; A/B=66-360.
DR PDB; 4AF6; X-ray; 2.90 A; A/B=53-360.
DR PDB; 4AF7; X-ray; 2.85 A; A/B=53-360.
DR PDBsum; 1QFY; -.
DR PDBsum; 1QFZ; -.
DR PDBsum; 1QG0; -.
DR PDBsum; 1QGA; -.
DR PDBsum; 2XNC; -.
DR PDBsum; 3MHP; -.
DR PDBsum; 4AF6; -.
DR PDBsum; 4AF7; -.
DR AlphaFoldDB; P10933; -.
DR SMR; P10933; -.
DR DIP; DIP-35575N; -.
DR IntAct; P10933; 3.
DR PRIDE; P10933; -.
DR EnsemblPlants; Psat2g154080.2; Psat2g154080.2.cds; Psat2g154080.
DR Gramene; Psat2g154080.2; Psat2g154080.2.cds; Psat2g154080.
DR BRENDA; 1.18.1.2; 4872.
DR BRENDA; 1.19.1.1; 4872.
DR SABIO-RK; P10933; -.
DR UniPathway; UPA00091; -.
DR EvolutionaryTrace; P10933; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; 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 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Electron transport; FAD; Flavoprotein; Membrane;
KW NADP; Oxidoreductase; Photosynthesis; Plastid; Thylakoid; Transit peptide;
KW Transport.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT CHAIN 53..360
FT /note="Ferredoxin--NADP reductase, leaf isozyme,
FT chloroplastic"
FT /id="PRO_0000019411"
FT DOMAIN 81..203
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 139..142
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 142
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 160..162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 166
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 177..179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 218
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 250..251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 280..281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 319..320
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10467097"
FT BINDING 358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:10467097"
FT MUTAGEN 360
FT /note="Y->F: Results in a 2.0-fold reduction in kcat for
FT the diaphorase reaction."
FT /evidence="ECO:0000269|PubMed:8366077"
FT MUTAGEN 360
FT /note="Y->G: Results in a 302-fold reduction in kcat for
FT the diaphorase reaction."
FT /evidence="ECO:0000269|PubMed:8366077"
FT MUTAGEN 360
FT /note="Y->S: Results in a 22-fold reduction in kcat for the
FT diaphorase reaction."
FT /evidence="ECO:0000269|PubMed:8366077"
FT MUTAGEN 360
FT /note="Y->W: Results in a 2.2-fold reduction in kcat for
FT the diaphorase reaction."
FT /evidence="ECO:0000269|PubMed:8366077"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1QFY"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3MHP"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2XNC"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3MHP"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4AF7"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 259..268
FT /evidence="ECO:0007829|PDB:1QFZ"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 273..279
FT /evidence="ECO:0007829|PDB:1QFZ"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 293..297
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 301..309
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 313..320
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 323..337
FT /evidence="ECO:0007829|PDB:1QFZ"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:1QFZ"
FT STRAND 355..360
FT /evidence="ECO:0007829|PDB:1QFZ"
SQ SEQUENCE 360 AA; 40194 MW; 7F1CC10DEBBA7B24 CRC64;
MAAAVTAAVS LPYSNSTSLP IRTSIVAPER LVFKKVSLNN VSISGRVGTI RAQVTTEAPA
KVVKHSKKQD ENIVVNKFKP KEPYVGRCLL NTKITGDDAP GETWHMVFST EGEVPYREGQ
SIGIVPDGID KNGKPHKLRL YSIASSAIGD FGDSKTVSLC VKRLVYTNDA GEVVKGVCSN
FLCDLKPGSE VKITGPVGKE MLMPKDPNAT VIMLGTGTGI APFRSFLWKM FFEKHEDYQF
NGLAWLFLGV PTSSSLLYKE EFEKMKEKAP ENFRLDFAVS REQVNDKGEK MYIQTRMAQY
AEELWELLKK DNTFVYMCGL KGMEKGIDDI MVSLAAKDGI DWIEYKRTLK KAEQWNVEVY
