FENR_NOSSO
ID FENR_NOSSO Reviewed; 440 AA.
AC P21890;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Ferredoxin--NADP reductase;
DE Short=FNR;
DE EC=1.18.1.2;
GN Name=petH;
OS Nostoc sp. (strain ATCC 29151 / PCC 7119) (Anabaena sp.).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=1168;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8343609; DOI=10.1007/bf00047415;
RA Fillat M.F., Flores E., Gomez-Moreno C.;
RT "Homology of the N-terminal domain of the petH gene product from Anabaena
RT sp. PCC 7119 to the CpcD phycobilisome linker polypeptide.";
RL Plant Mol. Biol. 22:725-729(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 137-440.
RX PubMed=2124680; DOI=10.1093/nar/18.23.7161;
RA Fillat M.F., Bakker H.A.C., Weisbeek P.J.;
RT "Sequence of the ferredoxin-NADP(+)-reductase gene from Anabaena PCC
RT 7119.";
RL Nucleic Acids Res. 18:7161-7161(1990).
RN [3]
RP PROTEIN SEQUENCE OF 152-183.
RC STRAIN=1403.46;
RX PubMed=3124746; DOI=10.1016/0003-9861(88)90441-9;
RA Sancho J., Peleato M.L., Gomez-Moreno C., Edmondson D.E.;
RT "Purification and properties of ferredoxin-NADP+ oxidoreductase from the
RT nitrogen-fixing cyanobacteria Anabaena variabilis.";
RL Arch. Biochem. Biophys. 260:200-207(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
RX PubMed=8890910; DOI=10.1006/jmbi.1996.0553;
RA Serre L., Vellieux F.M.D., Medina M., Gomez-Moreno C.,
RA Fontecilla-Camps J.-C., Frey M.;
RT "X-ray structure of the ferredoxin:NADP+ reductase from the cyanobacterium
RT Anabaena PCC 7119 at 1.8-A resolution, and crystallographic studies of
RT NADP+ binding at 2.25-A resolution.";
RL J. Mol. Biol. 263:20-39(1996).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 146-440.
RX PubMed=9922134; DOI=10.1021/bi981718i;
RA Martinez-Julvez M., Hermoso J., Hurley J.K., Mayoral T., Sanz-Aparicio J.,
RA Tollin G., Gomez-Moreno C., Medina M.;
RT "Role of Arg100 and Arg264 from Anabaena PCC 7119 ferredoxin-NADP+
RT reductase for optimal NADP+ binding and electron transfer.";
RL Biochemistry 37:17680-17691(1998).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 137-440.
RX PubMed=10651039;
RX DOI=10.1002/(sici)1097-0134(20000101)38:1<60::aid-prot7>3.0.co;2-b;
RA Mayoral T., Medina M., Sanz-Aparicio J., Gomez-Moreno C., Hermoso J.A.;
RT "Structural basis of the catalytic role of Glu301 in Anabaena PCC 7119
RT ferredoxin-NADP+ reductase revealed by X-ray crystallography.";
RL Proteins 38:60-69(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS).
RX PubMed=11053838; DOI=10.1107/s0907444900010052;
RA Morales R., Kachalova G., Vellieux F., Charon M.-H., Frey M.;
RT "Crystallographic studies of the interaction between the ferredoxin-NADP+
RT reductase and ferredoxin from the cyanobacterium Anabaena: looking for the
RT elusive ferredoxin molecule.";
RL Acta Crystallogr. D 56:1408-1412(2000).
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC -!- INTERACTION:
CC P21890; P0A3E0: isiB; NbExp=5; IntAct=EBI-593915, EBI-593907;
CC P21890; P0A3C8: petF; NbExp=5; IntAct=EBI-593915, EBI-637080;
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=May be bound to the thylakoid membrane
CC or anchored to the thylakoid-bound phycobilisomes.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X72394; CAA51088.1; -; Genomic_DNA.
DR EMBL; X54039; CAA37973.1; -; Genomic_DNA.
DR PDB; 1B2R; X-ray; 1.80 A; A=137-440.
DR PDB; 1BJK; X-ray; 2.30 A; A=146-440.
DR PDB; 1BQE; X-ray; 2.45 A; A=146-440.
DR PDB; 1E62; X-ray; 2.30 A; A=137-440.
DR PDB; 1E63; X-ray; 2.30 A; A=137-440.
DR PDB; 1E64; X-ray; 2.30 A; A=137-440.
DR PDB; 1EWY; X-ray; 2.38 A; A/B=138-440.
DR PDB; 1GJR; X-ray; 2.10 A; A=137-440.
DR PDB; 1GO2; X-ray; 1.70 A; A=137-440.
DR PDB; 1GR1; X-ray; 2.50 A; A=138-440.
DR PDB; 1H42; X-ray; 2.15 A; A=137-440.
DR PDB; 1H85; X-ray; 2.30 A; A=146-440.
DR PDB; 1OGI; X-ray; 1.64 A; A=138-440.
DR PDB; 1OGJ; X-ray; 1.64 A; A=138-440.
DR PDB; 1QGY; X-ray; 1.70 A; A=146-440.
DR PDB; 1QGZ; X-ray; 2.30 A; A=146-440.
DR PDB; 1QH0; X-ray; 1.93 A; A=146-440.
DR PDB; 1QUE; X-ray; 1.80 A; A=138-440.
DR PDB; 1QUF; X-ray; 2.25 A; A=137-440.
DR PDB; 1W34; X-ray; 1.73 A; A=137-440.
DR PDB; 1W35; X-ray; 1.90 A; A=137-440.
DR PDB; 1W87; X-ray; 3.00 A; A/B=137-440.
DR PDB; 2BMW; X-ray; 1.50 A; A=137-440.
DR PDB; 2BSA; X-ray; 1.92 A; A=138-440.
DR PDB; 2VYQ; X-ray; 1.90 A; A=137-440.
DR PDB; 2VZL; X-ray; 1.93 A; A=137-440.
DR PDB; 2X3U; X-ray; 1.93 A; A=138-440.
DR PDB; 3ZBT; X-ray; 1.92 A; A=138-440.
DR PDB; 3ZBU; X-ray; 1.89 A; A=138-440.
DR PDB; 3ZC3; X-ray; 2.30 A; A/B=138-440.
DR PDB; 4BPR; X-ray; 2.00 A; A=138-440.
DR PDB; 4C43; X-ray; 1.70 A; A=138-440.
DR PDBsum; 1B2R; -.
DR PDBsum; 1BJK; -.
DR PDBsum; 1BQE; -.
DR PDBsum; 1E62; -.
DR PDBsum; 1E63; -.
DR PDBsum; 1E64; -.
DR PDBsum; 1EWY; -.
DR PDBsum; 1GJR; -.
DR PDBsum; 1GO2; -.
DR PDBsum; 1GR1; -.
DR PDBsum; 1H42; -.
DR PDBsum; 1H85; -.
DR PDBsum; 1OGI; -.
DR PDBsum; 1OGJ; -.
DR PDBsum; 1QGY; -.
DR PDBsum; 1QGZ; -.
DR PDBsum; 1QH0; -.
DR PDBsum; 1QUE; -.
DR PDBsum; 1QUF; -.
DR PDBsum; 1W34; -.
DR PDBsum; 1W35; -.
DR PDBsum; 1W87; -.
DR PDBsum; 2BMW; -.
DR PDBsum; 2BSA; -.
DR PDBsum; 2VYQ; -.
DR PDBsum; 2VZL; -.
DR PDBsum; 2X3U; -.
DR PDBsum; 3ZBT; -.
DR PDBsum; 3ZBU; -.
DR PDBsum; 3ZC3; -.
DR PDBsum; 4BPR; -.
DR PDBsum; 4C43; -.
DR AlphaFoldDB; P21890; -.
DR SMR; P21890; -.
DR IntAct; P21890; 3.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR BRENDA; 1.18.1.2; 319.
DR BRENDA; 1.19.1.1; 4371.
DR EvolutionaryTrace; P21890; -.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; TAS:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; TAS:UniProtKB.
DR GO; GO:0050661; F:NADP binding; TAS:UniProtKB.
DR GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR008213; CpcD-like_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; PTHR43314; 1.
DR Pfam; PF01383; CpcD; 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 SMART; SM01094; CpcD; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51441; CPCD_LIKE; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antenna complex; Direct protein sequencing; FAD;
KW Flavoprotein; Membrane; NADP; Oxidoreductase; Phycobilisome; Thylakoid.
FT CHAIN 1..440
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000167632"
FT DOMAIN 17..75
FT /note="CpcD-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00771"
FT DOMAIN 155..279
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 99..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 214..217
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 217
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 235..237
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 237
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 253..255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT BINDING 294
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 330..331
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 360..361
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 370..374
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT BINDING 399..400
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 438
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT CONFLICT 180
FT /note="I -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:1EWY"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:1W87"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:2BMW"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1GJR"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1W87"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:2BMW"
FT TURN 222..227
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1W34"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1W34"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 339..348
FT /evidence="ECO:0007829|PDB:2BMW"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:2BMW"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 373..379
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 393..399
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 403..416
FT /evidence="ECO:0007829|PDB:2BMW"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:2BMW"
FT HELIX 422..431
FT /evidence="ECO:0007829|PDB:2BMW"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:2BMW"
SQ SEQUENCE 440 AA; 48865 MW; 8E1F61D0F09338B6 CRC64;
MSNQGAFDGA ANVESGSRVF VYEVVGMRQN EETDQTNYPI RKSGSVFIRV PYNRMNQEMQ
RITRLGGKIV TIQTVSALQQ LNGRTTIATV TDASSEIAKS EGNGKATPVK TDSGAKAFAK
PPAEEQLKKK DNKGNTMTQA KAKHADVPVN LYRPNAPFIG KVISNEPLVK EGGIGIVQHI
KFDLTGGNLK YIEGQSIGII PPGVDKNGKP EKLRLYSIAS TRHGDDVDDK TISLCVRQLE
YKHPESGETV YGVCSTYLTH IEPGSEVKIT GPVGKEMLLP DDPEANVIML ATGTGIAPMR
TYLWRMFKDA ERAANPEYQF KGFSWLVFGV PTTPNILYKE ELEEIQQKYP DNFRLTYAIS
REQKNPQGGR MYIQDRVAEH ADELWQLIKN QKTHTYICGL RGMEEGIDAA LSAAAAKEGV
TWSDYQKDLK KAGRWHVETY
