ID   Q9SLP5_MAIZE            Unreviewed;       368 AA.
AC   Q9SLP5;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 149.
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   Name=L-FNRII {ECO:0000313|EMBL:BAA88237.1};
GN   Synonyms=541626 {ECO:0000313|EnsemblPlants:Zm00001eb140530_P001};
GN   ORFNames=ZEAMMB73_Zm00001d042049 {ECO:0000313|EMBL:ONM34374.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:BAA88237.1};
RN   [1] {ECO:0000313|EMBL:BAA88237.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:BAA88237.1};
RX   PubMed=10889253; DOI=10.1104/pp.123.3.1037;
RA   Onda Y., Matsumura T., Kimata-Ariga Y., Sakakibara H., Sugiyama T.,
RA   Hase T.;
RT   "Differential interaction of maize root ferredoxin:NADP(+) oxidoreductase
RT   with photosynthetic and non-photosynthetic ferredoxin isoproteins.";
RL   Plant Physiol. 123:1037-1045(2000).
RN   [2] {ECO:0007829|PDB:3VO1}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 56-368 IN COMPLEX WITH FAD.
RX   PubMed=22805436; DOI=10.1105/tpc.111.094532;
RA   Twachtmann M., Altmann B., Muraki N., Voss I., Okutani S., Kurisu G.,
RA   Hase T., Hanke G.T.;
RT   "N-terminal structure of maize ferredoxin:NADP+ reductase determines
RT   recruitment into different thylakoid membrane complexes.";
RL   Plant Cell 24:2979-2991(2012).
RN   [3] {ECO:0000313|EMBL:ONM34374.1, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb140530_P001,
RC   ECO:0000313|Proteomes:UP000007305};
RC   TISSUE=Seedling {ECO:0000313|EMBL:ONM34374.1};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EnsemblPlants:Zm00001eb140530_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb140530_P001};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
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
CC       {ECO:0000256|PIRNR:PIRNR000361}.
CC   -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008312, ECO:0000256|PIRNR:PIRNR000361}.
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DR   EMBL; AB035645; BAA88237.1; -; mRNA.
DR   EMBL; CM007649; ONM34374.1; -; Genomic_DNA.
DR   EMBL; CM007649; ONM34376.1; -; Genomic_DNA.
DR   EMBL; CM007649; ONM34377.1; -; Genomic_DNA.
DR   RefSeq; NP_001104851.1; NM_001111381.1.
DR   PDB; 3VO1; X-ray; 2.00 A; A/B=56-368.
DR   PDBsum; 3VO1; -.
DR   PaxDb; 4577-GRMZM2G059083_P01; -.
DR   EnsemblPlants; Zm00001eb140530_T001; Zm00001eb140530_P001; Zm00001eb140530.
DR   EnsemblPlants; Zm00001eb140530_T002; Zm00001eb140530_P002; Zm00001eb140530.
DR   EnsemblPlants; Zm00001eb140530_T005; Zm00001eb140530_P005; Zm00001eb140530.
DR   GeneID; 541626; -.
DR   Gramene; Zm00001eb140530_T001; Zm00001eb140530_P001; Zm00001eb140530.
DR   Gramene; Zm00001eb140530_T002; Zm00001eb140530_P002; Zm00001eb140530.
DR   Gramene; Zm00001eb140530_T005; Zm00001eb140530_P005; Zm00001eb140530.
DR   KEGG; zma:541626; -.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_053066_0_0_1; -.
DR   OMA; ATIIMEF; -.
DR   OrthoDB; 287at2759; -.
DR   UniPathway; UPA00091; -.
DR   Proteomes; UP000007305; Chromosome 3.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniPathway.
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:SF25; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:3VO1};
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   Nucleotide-binding {ECO:0007829|PDB:3VO1};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000361};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9SLP5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305}.
FT   DOMAIN          89..211
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         147
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         148
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         150
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         150
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         168
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         170
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         170
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         174
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         185
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         186
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         187
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0007829|PDB:3VO1"
FT   BINDING         226
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         258..259
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         288..289
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         298
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         327..328
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         366
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ   SEQUENCE   368 AA;  40864 MW;  6F9DEBD77DC6C338 CRC64;
     MAAVTAAAVS LPSSSSSPAA AKAKASASAS PSSPCGHLQF PRRHGGPRAV RLRVQVSTTE
     TAEAEPVKKL EKVSKKQEEG LVTNKYKPKE PYVGRCLLNT RITGDQAPGE TWHMVFSTEG
     EVPYREGQSI GVIADGEDKN GKPHKLRLYS IASSALGDFG DSKTVSLCVK RLVYTNDQGE
     VVKGVCSNFL CDLKPGAEVK ITGPVGKEML MPKDPNATII MLATGTGIAP FRSFLWKMFF
     EEHEDYKYTG LAWLFLGVPT SDTLLYKEEL EKMKEMAPDN FRLDFAVSRE QTNAAGEKMY
     IQTRMAEYKE ELWELLKKDN TYVYMCGLKG MEKGIDDIML DLAAKDGINW LDYKKQLKKS
     EQWNVEVY
//