ID   Q9SLP6_MAIZE            Unreviewed;       355 AA.
AC   Q9SLP6; A0A3L6DH98;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 172.
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-FNRI {ECO:0000313|EMBL:BAA88236.1};
GN   ORFNames=ZEAMMB73_Zm00001d045575 {ECO:0000313|EMBL:AQL02647.1};
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:BAA88236.1};
RN   [1] {ECO:0000313|EMBL:BAA88236.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:BAA88236.1};
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:1GAQ, ECO:0007829|PDB:1GAW}
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 42-355 IN COMPLEX WITH FAD.
RX   PubMed=11175898; DOI=10.1038/84097;
RA   Kurisu G., Kusunoki M., Katoh E., Yamazaki T., Teshima K., Onda Y.,
RA   Kimata-Ariga Y., Hase T.;
RT   "Structure of the electron transfer complex between ferredoxin and
RT   ferredoxin-NADP+ reductase.";
RL   Nat. Struct. Biol. 8:117-121(2001).
RN   [3] {ECO:0000313|EMBL:ACG31602.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [4] {ECO:0000313|EMBL:ACL53609.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACL53609.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [5] {ECO:0000313|EnsemblPlants:Zm00001eb379240_P002, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb379240_P002,
RC   ECO:0000313|Proteomes:UP000007305};
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA   Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA   Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA   Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA   Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA   Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA   Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA   Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA   Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA   Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA   Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA   Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA   SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA   Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA   Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA   Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA   Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA   Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
RN   [6] {ECO:0007829|PDB:3W5U, ECO:0007829|PDB:3W5V}
RP   X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 42-355 IN COMPLEX WITH FAD.
RX   PubMed=23618857; DOI=10.1016/j.bbrc.2013.04.033;
RA   Kimata-Ariga Y., Kubota-Kawai H., Lee Y.H., Muraki N., Ikegami T.,
RA   Kurisu G., Hase T.;
RT   "Concentration-dependent oligomerization of cross-linked complexes between
RT   ferredoxin and ferredoxin-NADP+ reductase.";
RL   Biochem. Biophys. Res. Commun. 434:867-872(2013).
RN   [7] {ECO:0000313|EMBL:AQL02647.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Seedling {ECO:0000313|EMBL:AQL02647.1};
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   [8] {ECO:0000313|EnsemblPlants:Zm00001eb379240_P002}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb379240_P002};
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 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   ---------------------------------------------------------------------------
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; EU959484; ACG31602.1; -; mRNA.
DR   EMBL; BT055002; ACL53609.1; -; mRNA.
DR   EMBL; CM000785; AQL02647.1; -; Genomic_DNA.
DR   EMBL; AB035644; BAA88236.1; -; mRNA.
DR   RefSeq; NP_001105568.1; NM_001112098.1.
DR   RefSeq; XP_008659023.1; XM_008660801.1.
DR   PDB; 1GAQ; X-ray; 2.59 A; A/C=42-355.
DR   PDB; 1GAW; X-ray; 2.20 A; A/B=42-355.
DR   PDB; 3W5U; X-ray; 2.70 A; A/C/E/G=42-355.
DR   PDB; 3W5V; X-ray; 3.81 A; A/C=42-355.
DR   PDBsum; 1GAQ; -.
DR   PDBsum; 1GAW; -.
DR   PDBsum; 3W5U; -.
DR   PDBsum; 3W5V; -.
DR   IntAct; Q9SLP6; 1.
DR   STRING; 4577.Q9SLP6; -.
DR   PaxDb; 4577-GRMZM2G168143_P01; -.
DR   EnsemblPlants; Zm00001eb379240_T002; Zm00001eb379240_P002; Zm00001eb379240.
DR   Gramene; Zm00001eb379240_T002; Zm00001eb379240_P002; Zm00001eb379240.
DR   eggNOG; KOG1158; Eukaryota.
DR   HOGENOM; CLU_053066_0_0_1; -.
DR   OMA; CVKRHRY; -.
DR   OrthoDB; 287at2759; -.
DR   BRENDA; 1.18.1.2; 6752.
DR   UniPathway; UPA00091; -.
DR   Proteomes; UP000007305; Chromosome 9.
DR   GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR   GO; GO:0098807; C:chloroplast thylakoid membrane protein complex; IBA:GO_Central.
DR   GO; GO:0009055; F:electron transfer activity; IDA:AgBase.
DR   GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003959; F:NADPH dehydrogenase activity; IDA:AgBase.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IDA:AgBase.
DR   GO; GO:0022900; P:electron transport chain; IDA:AgBase.
DR   GO; GO:0015979; P:photosynthesis; IC:AgBase.
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; IPR008333; Cbr1-like_FAD-bd_dom.
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; PF00970; FAD_binding_6; 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:1GAQ, ECO:0007829|PDB:1GAW};
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:1GAQ, ECO:0007829|PDB:1GAW};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000361};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q9SLP6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT   DOMAIN          76..198
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         134
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:1GAW"
FT   BINDING         134
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         135
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:1GAW"
FT   BINDING         135
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         136
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:3W5U"
FT   BINDING         137
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         137
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:1GAW"
FT   BINDING         137
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         155
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:1GAW"
FT   BINDING         155
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         157
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:1GAW"
FT   BINDING         157
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         157
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         161
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:3W5U"
FT   BINDING         161
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         172
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         172
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:1GAW"
FT   BINDING         173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:1GAW"
FT   BINDING         173
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         174
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0007829|PDB:1GAQ, ECO:0007829|PDB:1GAW"
FT   BINDING         174
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0007829|PDB:3W5V"
FT   BINDING         213
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         245..246
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         275..276
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         314..315
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT   BINDING         353
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ   SEQUENCE   355 AA;  39323 MW;  AE56B6A6BF471267 CRC64;
     MATVMAAAVS SFPSSSAVVA KASPASPCAA PHFRPRAVRA AIRAQASAVE APATAKAKKE
     SKKQEEGVVT NLYKPKEPYV GRCLLNTKIT GDDAPGETWH MVFSTEGKIP YREGQSIGVI
     ADGVDKNGKP HKVRLYSIAS SAIGDFGDSK TVSLCVKRLI YTNDAGEIVK GVCSNFLCDL
     QPGDNVQITG PVGKEMLMPK DPNATIIMLA TGTGIAPFRS FLWKMFFEKH DDYKFNGLGW
     LFLGVPTSSS LLYKEEFGKM KERAPENFRV DYAVSREQTN AAGERMYIQT RMAEYKEELW
     ELLKKDNTYV YMCGLKGMEK GIDDIMVSLA EKDGIDWFDY KKQLKRGDQW NVEVY
//