FENR_VICFA
ID FENR_VICFA Reviewed; 363 AA.
AC P41346;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Ferredoxin--NADP reductase, chloroplastic;
DE Short=FNR;
DE EC=1.18.1.2;
DE Flags: Precursor;
GN Name=PETH;
OS Vicia faba (Broad bean) (Faba vulgaris).
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; Vicia.
OX NCBI_TaxID=3906;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RA Lax A.R., Cary J.W.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; U14956; AAA21758.1; -; mRNA.
DR AlphaFoldDB; P41346; -.
DR SMR; P41346; -.
DR UniPathway; UPA00091; -.
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 2: Evidence at transcript level;
KW Chloroplast; Electron transport; FAD; Flavoprotein; Membrane; NADP;
KW Oxidoreductase; Photosynthesis; Plastid; Thylakoid; Transit peptide;
KW Transport.
FT TRANSIT 1..52
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..363
FT /note="Ferredoxin--NADP reductase, chloroplastic"
FT /id="PRO_0000019410"
FT DOMAIN 84..206
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 142..145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 163..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 180..182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 253..254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 283..284
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 322..323
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 40579 MW; CB0C8CC6D3203063 CRC64;
MAAAVTAAVS LPYSNSTSLP IRTSIVAPER LVFKKVSLNS VSISGRVGTI RAQITTEAEA
PVTKVVKHSK KQDEGIVVNK FKPKEPYVGR CLLNTKITGD DAPGETWHMV FTTEGEVPYR
EGQSIGIVPD GIDKNGKPHK LRLYSIASSA IGDFGDSKTV SLCVKRLVYT NDAGEVVKGV
CSNFLCDLKP GSEVKITGPV GKEMLMPKDP NATVIMLGTG TGIAPFRSFL WKMFFEKHED
YKFNGLAWLF LGVPTSSSLL YKEEFEKMKE KAPENFRLDF AVSREQVNDK GEKMYIQTRM
AQYAEELWEL LKKDNTFVYM CGLKGMEKGI DDIMVSIRPK DGIDWIEYKR TLKKAEQWNV
EVY
