FENR_AZOVI
ID FENR_AZOVI Reviewed; 258 AA.
AC Q44532;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ferredoxin--NADP reductase {ECO:0000305};
DE Short=FNR {ECO:0000305};
DE EC=1.18.1.2 {ECO:0000269|PubMed:8034707};
DE AltName: Full=NADPH:ferredoxin reductase {ECO:0000303|PubMed:7673160};
DE AltName: Full=Protein X {ECO:0000303|PubMed:8034707};
GN Name=fpr {ECO:0000303|PubMed:7673160};
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=7673160; DOI=10.1074/jbc.270.36.21258;
RA Isas J.M., Yannone S.M., Burgess B.K.;
RT "Azotobacter vinelandii NADPH:ferredoxin reductase cloning, sequencing, and
RT overexpression.";
RL J. Biol. Chem. 270:21258-21263(1995).
RN [2]
RP PROTEIN SEQUENCE OF 1-36, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP SUBUNIT.
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=8034707; DOI=10.1016/s0021-9258(17)32183-x;
RA Isas J.M., Burgess B.K.;
RT "Purification and characterization of a NADP+/NADPH-specific flavoprotein
RT that is overexpressed in FdI-strains of Azotobacter vinelandii.";
RL J. Biol. Chem. 269:19404-19409(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH FAD, AND COFACTOR.
RC STRAIN=LM100;
RX PubMed=9865948; DOI=10.1002/pro.5560071207;
RA Prasad G.S., Kresge N., Muhlberg A.B., Shaw A., Jung Y.S., Burgess B.K.,
RA Stout C.D.;
RT "The crystal structure of NADPH:ferredoxin reductase from Azotobacter
RT vinelandii.";
RL Protein Sci. 7:2541-2549(1998).
CC -!- FUNCTION: Transports electrons between ferredoxin and NADPH.
CC {ECO:0000269|PubMed:8034707}.
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:0000269|PubMed:8034707};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:8034707, ECO:0000269|PubMed:9865948};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8034707}.
CC -!- INDUCTION: Overexpressed under N(2)-fixing conditions.
CC {ECO:0000269|PubMed:7673160}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; L36319; AAA83029.1; -; Genomic_DNA.
DR PIR; A57432; A57432.
DR RefSeq; WP_012702363.1; NZ_FPKM01000003.1.
DR PDB; 1A8P; X-ray; 2.00 A; A=1-258.
DR PDBsum; 1A8P; -.
DR AlphaFoldDB; Q44532; -.
DR SMR; Q44532; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR PRIDE; Q44532; -.
DR OMA; MICGSSA; -.
DR EvolutionaryTrace; Q44532; -.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd06195; FNR1; 1.
DR Gene3D; 3.40.50.80; -; 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; IPR033892; FNR_bac.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00970; FAD_binding_6; 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; Direct protein sequencing; FAD; Flavoprotein; NADP;
KW Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..258
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000167639"
FT DOMAIN 2..102
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 51..54
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9865948"
FT BINDING 67..69
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9865948"
FT BINDING 74..77
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9865948"
FT BINDING 117
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9865948"
FT BINDING 144..145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 181..182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 190
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P28861"
FT BINDING 254..258
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:9865948"
FT STRAND 4..16
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1A8P"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 167..173
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:1A8P"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:1A8P"
FT HELIX 222..234
FT /evidence="ECO:0007829|PDB:1A8P"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:1A8P"
SQ SEQUENCE 258 AA; 29417 MW; 2865C2FC786A6C04 CRC64;
MSNLNVERVL SVHHWNDTLF SFKTTRNPSL RFENGQFVMI GLEVDGRPLM RAYSIASPNY
EEHLEFFSIK VQNGPLTSRL QHLKEGDELM VSRKPTGTLV TSDLLPGKHL YMLSTGTGLA
PFMSLIQDPE VYERFEKVVL IHGVRQVNEL AYQQFITEHL PQSEYFGEAV KEKLIYYPTV
TRESFHNQGR LTDLMRSGKL FEDIGLPPIN PQDDRAMICG SPSMLDESCE VLDGFGLKIS
PRMGEPGDYL IERAFVEK
