ID A4S9W0_OSTLU Unreviewed; 360 AA.
AC A4S9W0;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Ferredoxin--NADP reductase, chloroplastic {ECO:0000256|PIRNR:PIRNR000361};
DE Short=FNR {ECO:0000256|PIRNR:PIRNR000361};
DE EC=1.18.1.2 {ECO:0000256|PIRNR:PIRNR000361};
GN ORFNames=OSTLU_28333 {ECO:0000313|EMBL:ABP00557.1};
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABP00557.1, ECO:0000313|Proteomes:UP000001568};
RN [1] {ECO:0000313|EMBL:ABP00557.1, ECO:0000313|Proteomes:UP000001568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABP00557.1,
RC ECO:0000313|Proteomes:UP000001568};
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
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:0000256|ARBA:ARBA00001005,
CC ECO:0000256|PIRNR:PIRNR000361};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Energy metabolism; photosynthesis.
CC {ECO:0000256|ARBA:ARBA00004748}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000256|ARBA:ARBA00004185}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004185}; Stromal side
CC {ECO:0000256|ARBA:ARBA00004185}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312, ECO:0000256|PIRNR:PIRNR000361}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000597; ABP00557.1; -; Genomic_DNA.
DR RefSeq; XP_001422240.1; XM_001422203.1.
DR AlphaFoldDB; A4S9W0; -.
DR STRING; 436017.A4S9W0; -.
DR EnsemblPlants; ABP00557; ABP00557; OSTLU_28333.
DR GeneID; 5006297; -.
DR Gramene; ABP00557; ABP00557; OSTLU_28333.
DR KEGG; olu:OSTLU_28333; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_053066_1_0_1; -.
DR OMA; CHIIIEH; -.
DR OrthoDB; 287at2759; -.
DR Proteomes; UP000001568; Chromosome 17.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR CDD; cd06208; CYPOR_like_FNR; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; -; 1.
DR PANTHER; PTHR43314:SF27; FERREDOXIN--NADP REDUCTASE, LEAF ISOZYME 2, CHLOROPLASTIC; 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; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000361};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000361};
KW NADP {ECO:0000256|PIRNR:PIRNR000361, ECO:0000256|PIRSR:PIRSR000361-1};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000361};
KW Reference proteome {ECO:0000313|Proteomes:UP000001568};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 74..204
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 139
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 159
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 219
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 281..282
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 319..320
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ SEQUENCE 360 AA; 39924 MW; 189D5A02D730962A CRC64;
MALTVSAFAG AKINAARQTK ARRATAVVRA EGTDYGLGLQ CSPTANKNID PKGRAKVPLE
LEDMPLPLNT FKNKEPFTGK VRSVERIVGP NATGETCHII IEHGGKMPFW EGQSYGVIPP
GTKVNSKGKE VPHGVRLYSI ASSRYGDSYD GQTATLCVRR ATYWDPEMNA EDPAKKGICS
NFLCDAKPGA EVMMTGPTGQ VMLLPKDPAT PVIMVATGTG IAPMRSYIRR FFLEDVPNWE
FKGLAWLFMG VANSDAKLYD DEFQECAKRF PDQFRIDYAL SREDTNKNGG KMYIQDKVEE
YKDQVFQLLD GGAHMYFCGL KGMMPGILSM LEGVCKEKGI SYEEWLEGLK KKGQWHVEVY
//
