FENR_PLAF7
ID FENR_PLAF7 Reviewed; 371 AA.
AC C6KT68;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ferredoxin--NADP reductase, apicoplast {ECO:0000303|PubMed:17251200, ECO:0000303|PubMed:17258767, ECO:0000303|PubMed:19736991};
DE EC=1.18.1.2 {ECO:0000305|PubMed:16289098, ECO:0000305|PubMed:17251200, ECO:0000305|PubMed:17258767, ECO:0000305|PubMed:19736991};
DE Flags: Precursor;
GN Name=FNR {ECO:0000303|PubMed:16289098};
GN ORFNames=PF3D7_0623200 {ECO:0000312|EMBL:CAG25044.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|EMBL:CAG25044.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16289098; DOI=10.1016/j.febslet.2005.10.037;
RA Roehrich R.C., Englert N., Troschke K., Reichenberg A., Hintz M.,
RA Seeber F., Balconi E., Aliverti A., Zanetti G., Koehler U., Pfeiffer M.,
RA Beck E., Jomaa H., Wiesner J.;
RT "Reconstitution of an apicoplast-localised electron transfer pathway
RT involved in the isoprenoid biosynthesis of Plasmodium falciparum.";
RL FEBS Lett. 579:6433-6438(2005).
RN [4]
RP CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=17251200; DOI=10.1093/jb/mvm046;
RA Kimata-Ariga Y., Kurisu G., Kusunoki M., Aoki S., Sato D., Kobayashi T.,
RA Kita K., Horii T., Hase T.;
RT "Cloning and characterization of ferredoxin and ferredoxin-NADP+ reductase
RT from human malaria parasite.";
RL J. Biochem. 141:421-428(2007).
RN [5] {ECO:0007744|PDB:2OK7, ECO:0007744|PDB:2OK8}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 56-371 IN COMPLEX WITH FAD AND
RP THE NADP ANALOG ADENOSINE-2'-5'-DIPHOSPHATE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, AND DISULFIDE BOND.
RX PubMed=17258767; DOI=10.1016/j.jmb.2007.01.005;
RA Milani M., Balconi E., Aliverti A., Mastrangelo E., Seeber F.,
RA Bolognesi M., Zanetti G.;
RT "Ferredoxin-NADP+ reductase from Plasmodium falciparum undergoes NADP+-
RT dependent dimerization and inactivation: functional and crystallographic
RT analysis.";
RL J. Mol. Biol. 367:501-513(2007).
RN [6] {ECO:0007744|PDB:3JQP, ECO:0007744|PDB:3JQQ, ECO:0007744|PDB:3JQR}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 56-371 IN COMPLEX WITH FAD AND
RP THE NADP ANALOG ADENOSINE-2'-5'-DIPHOSPHATE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT, MUTAGENESIS OF LYS-304
RP AND HIS-341, AND DISULFIDE BOND.
RX PubMed=19736991; DOI=10.1021/bi9013209;
RA Crobu D., Canevari G., Milani M., Pandini V., Vanoni M.A., Bolognesi M.,
RA Zanetti G., Aliverti A.;
RT "Plasmodium falciparum ferredoxin-NADP+ reductase His286 plays a dual role
RT in NADP(H) binding and catalysis.";
RL Biochemistry 48:9525-9533(2009).
CC -!- FUNCTION: May play a role in the terminal step of the DOXP/MEP pathway
CC for isoprenoid precursor biosynthesis. {ECO:0000269|PubMed:16289098}.
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:0000305|PubMed:16289098, ECO:0000305|PubMed:17251200,
CC ECO:0000305|PubMed:17258767, ECO:0000305|PubMed:19736991};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17251200, ECO:0000269|PubMed:17258767,
CC ECO:0000269|PubMed:19736991};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=36 uM for NADPH {ECO:0000269|PubMed:17258767,
CC ECO:0000269|PubMed:19736991};
CC KM=720 uM for NADH {ECO:0000269|PubMed:17258767};
CC -!- SUBUNIT: Monomer (PubMed:17258767). Homodimer; disulfide linked
CC (PubMed:17258767, PubMed:19736991). NADP binding accelerates formation
CC of an inactive, disulfide-linked homodimer when the protein is exposed
CC to air for 24 h or more (in vitro); the physiological relevance of this
CC is uncertain (PubMed:17258767). {ECO:0000269|PubMed:17258767,
CC ECO:0000269|PubMed:19736991}.
CC -!- INTERACTION:
CC C6KT68; Q8IED5: FD; NbExp=3; IntAct=EBI-7046197, EBI-7046314;
CC C6KT68; C6KT68: FNR; NbExp=2; IntAct=EBI-7046197, EBI-7046197;
CC -!- SUBCELLULAR LOCATION: Plastid, apicoplast {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; AL844505; CAG25044.1; -; Genomic_DNA.
DR RefSeq; XP_966214.1; XM_961121.1.
DR PDB; 2OK7; X-ray; 2.70 A; A/B/C/D/E/F=56-371.
DR PDB; 2OK8; X-ray; 2.40 A; A/B/C/D=56-371.
DR PDB; 3JQP; X-ray; 3.00 A; A/B/C/D/E/F=56-371.
DR PDB; 3JQQ; X-ray; 2.20 A; A/B/C/D/E/F=56-371.
DR PDB; 3JQR; X-ray; 2.30 A; A=56-371.
DR PDBsum; 2OK7; -.
DR PDBsum; 2OK8; -.
DR PDBsum; 3JQP; -.
DR PDBsum; 3JQQ; -.
DR PDBsum; 3JQR; -.
DR AlphaFoldDB; C6KT68; -.
DR SMR; C6KT68; -.
DR IntAct; C6KT68; 1.
DR MINT; C6KT68; -.
DR STRING; 5833.PFF1115w; -.
DR DrugBank; DB06608; Tafenoquine.
DR PRIDE; C6KT68; -.
DR EnsemblProtists; CAG25044; CAG25044; PF3D7_0623200.
DR GeneID; 3885862; -.
DR KEGG; pfa:PF3D7_0623200; -.
DR VEuPathDB; PlasmoDB:PF3D7_0623200; -.
DR HOGENOM; CLU_755410_0_0_1; -.
DR InParanoid; C6KT68; -.
DR OMA; RPRHVNK; -.
DR PhylomeDB; C6KT68; -.
DR BRENDA; 1.18.1.2; 4889.
DR SABIO-RK; C6KT68; -.
DR EvolutionaryTrace; C6KT68; -.
DR Proteomes; UP000001450; Chromosome 6.
DR GO; GO:0020011; C:apicoplast; IDA:GeneDB.
DR GO; GO:0009055; F:electron transfer activity; IDA:GeneDB.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0008937; F:ferredoxin-NAD(P) reductase activity; IDA:UniProtKB.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0010322; P:regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IDA:UniProtKB.
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; 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 PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apicoplast; Disulfide bond; Electron transport; FAD;
KW Flavoprotein; NADP; Nucleotide-binding; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..18
FT /note="Apicoplast"
FT /evidence="ECO:0000255"
FT CHAIN 19..371
FT /note="Ferredoxin--NADP reductase, apicoplast"
FT /id="PRO_5002968039"
FT DOMAIN 68..218
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 68
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17258767,
FT ECO:0007744|PDB:2OK8"
FT BINDING 155..159
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17258767,
FT ECO:0000269|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:2OK8, ECO:0007744|PDB:3JQP,
FT ECO:0007744|PDB:3JQQ, ECO:0007744|PDB:3JQR"
FT BINDING 172..179
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17258767,
FT ECO:0000269|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:2OK8, ECO:0007744|PDB:3JQP,
FT ECO:0007744|PDB:3JQQ, ECO:0007744|PDB:3JQR"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:17258767,
FT ECO:0000305|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:3JQP, ECO:0007744|PDB:3JQQ"
FT BINDING 192..194
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17258767,
FT ECO:0000269|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:2OK8, ECO:0007744|PDB:3JQP,
FT ECO:0007744|PDB:3JQQ, ECO:0007744|PDB:3JQR"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19736991,
FT ECO:0007744|PDB:3JQP"
FT BINDING 272..273
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:17258767,
FT ECO:0000305|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:3JQP"
FT BINDING 302
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:17258767,
FT ECO:0000305|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:3JQP, ECO:0007744|PDB:3JQQ"
FT BINDING 313..315
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:17258767,
FT ECO:0000305|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:3JQP, ECO:0007744|PDB:3JQQ"
FT BINDING 341..343
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000305|PubMed:17258767,
FT ECO:0000305|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:3JQP, ECO:0007744|PDB:3JQQ"
FT BINDING 342
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:19736991,
FT ECO:0007744|PDB:3JQQ"
FT BINDING 371
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:17258767,
FT ECO:0000269|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:2OK8, ECO:0007744|PDB:3JQP,
FT ECO:0007744|PDB:3JQQ, ECO:0007744|PDB:3JQR"
FT DISULFID 154
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:17258767,
FT ECO:0000269|PubMed:19736991, ECO:0007744|PDB:2OK7,
FT ECO:0007744|PDB:2OK8, ECO:0007744|PDB:3JQP,
FT ECO:0007744|PDB:3JQR"
FT MUTAGEN 304
FT /note="K->A: Slightly decreases affinity for NADPH."
FT /evidence="ECO:0000269|PubMed:19736991"
FT MUTAGEN 341
FT /note="H->A,L: Strongly decreases affinity for NADPH."
FT /evidence="ECO:0000269|PubMed:19736991"
FT MUTAGEN 341
FT /note="H->K: Strongly decreases catalytic activity.
FT Abolishes NADPH binding."
FT /evidence="ECO:0000269|PubMed:19736991"
FT MUTAGEN 341
FT /note="H->Q: Increases catalytic activity. Slightly
FT decreases affinity for NADPH."
FT /evidence="ECO:0000269|PubMed:19736991"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 71..80
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 238..247
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 281..290
FT /evidence="ECO:0007829|PDB:3JQQ"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:2OK7"
FT HELIX 314..320
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 322..331
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 335..340
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:3JQQ"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:3JQQ"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3JQQ"
SQ SEQUENCE 371 AA; 43779 MW; 971B66E201FB352D CRC64;
MKIRFVFILS VLISGVCCIS KNVSRRVANR MTAHSRFLFV HDKYKRNKNF KLKNNKEENN
FINLYTVKNP LKCKIVDKIN LVRPNSPNEV YHLEINHNGL FKYLEGHTCG IIPYYNELDN
NPNNQINKDH NIINTTNHTN HNNIALSHIK KQRCARLYSI SSSNNMENLS VAIKIHKYEQ
TENAPNITNY GYCSGFIKNL KINDDIYLTG AHGYFNLPND AIQKNTNFIF IATGTGISPY
ISFLKKLFAY DKNNLYNRNS NYTGYITIYY GVYNEDSILY LNELEYFQKM YPNNINIHYV
FSYKQNSDAT SFYVQDEIYK RKTEFLNLFN NYKCELYICG HKSIRYKVMD ILKSHDQFDE
KKKKRVHVEV Y
