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Database: UniProt
Entry: A0A2J6M973_LACSA
LinkDB: A0A2J6M973_LACSA
Original site: A0A2J6M973_LACSA 
ID   A0A2J6M973_LACSA        Unreviewed;       362 AA.
AC   A0A2J6M973;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=LSAT_3X73300 {ECO:0000313|EMBL:PLY96142.1};
OS   Lactuca sativa (Garden lettuce).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Cichorioideae; Cichorieae;
OC   Lactucinae; Lactuca.
OX   NCBI_TaxID=4236 {ECO:0000313|EMBL:PLY96142.1};
RN   [1] {ECO:0000313|EMBL:PLY96142.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=28401891; DOI=10.1038/ncomms14953;
RA   Reyes-Chin-Wo S., Wang Z., Yang X., Kozik A., Arikit S., Song C., Xia L.,
RA   Froenicke L., Lavelle D.O., Truco M.J., Xia R., Zhu S., Xu C., Xu H.,
RA   Xu X., Cox K., Korf I., Meyers B.C., Michelmore R.W.;
RT   "Genome assembly with in vitro proximity ligation data and whole-genome
RT   triplication in lettuce.";
RL   Nat. Commun. 8:14953-14953(2017).
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 stroma
CC       {ECO:0000256|ARBA:ARBA00004470}. Plastid, chloroplast thylakoid
CC       membrane {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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PLY96142.1}.
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DR   EMBL; NBSK01000841; PLY96142.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6M973; -.
DR   STRING; 4236.A0A2J6M973; -.
DR   EnsemblPlants; rna-gnl|WGS:NBSK|LSAT_3X73300_mrna; cds-PLY96142.1; gene-LSAT_3X73300.
DR   Gramene; rna-gnl|WGS:NBSK|LSAT_3X73300_mrna; cds-PLY96142.1; gene-LSAT_3X73300.
DR   OrthoDB; 287at2759; -.
DR   GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; IBA:GO_Central.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003959; F:NADPH dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
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 1, 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   Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT   DOMAIN          82..205
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         144
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         164
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         220
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         252..253
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         282..283
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         292
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         321..322
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         360
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ   SEQUENCE   362 AA;  40552 MW;  CD61A0C9B2950FEF CRC64;
     MASAVSAIVS LPSSKSAAIS TRTSLITQER VSFTKVPYYK NVSSNVKSLS IRAQVTTEAP
     AKVEKISKKQ EEGVVTNKYR PKEPYVGRCL LNTKITGDDA PGETWHMVFT TEGEIPYKEG
     QSIGVIPDGI DPKNGKPHKL RLYSIASSAL GDFGDSKTVS LCVKRLVYTN DAGEEVKGVC
     SNFLCDLKPG AEVQITGPVG KEMLMPKDPN ATVIMLATGT GIAPFRSFMW KMFFEKHEDY
     KFNGLAWLFL GVPTSSSLLY KEEFEKMKEM KPDNLRVDFA VSREQTNEKG EKMYIQTRMA
     QYDRELWELL KKDNTFVYMC GLKGMEKGID DIMGTLAAED GIDWVTYKKQ LKKEGQWNVE
     VY
//
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