FENR_RHOCA
ID FENR_RHOCA Reviewed; 270 AA.
AC Q9L6V3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Flavodoxin/ferredoxin--NADP reductase {ECO:0000305};
DE EC=1.18.1.2 {ECO:0000269|PubMed:14572660, ECO:0000269|PubMed:24016470};
DE EC=1.19.1.1 {ECO:0000269|PubMed:14572660, ECO:0000269|PubMed:16128574, ECO:0000269|PubMed:24016470};
DE AltName: Full=Ferredoxin (flavodoxin):NADP(+) oxidoreductase {ECO:0000305};
DE AltName: Full=Ferredoxin--NADP reductase {ECO:0000305};
DE Short=FNR {ECO:0000305};
DE AltName: Full=Flavodoxin--NADP reductase {ECO:0000305};
DE Short=FLDR {ECO:0000305};
GN Name=fpr {ECO:0000303|PubMed:14572660};
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-6, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=14572660; DOI=10.1016/s0014-5793(03)01075-5;
RA Bittel C., Tabares L.C., Armesto M., Carrillo N., Cortez N.;
RT "The oxidant-responsive diaphorase of Rhodobacter capsulatus is a
RT ferredoxin (flavodoxin)-NADP(H) reductase.";
RL FEBS Lett. 553:408-412(2003).
RN [2] {ECO:0007744|PDB:2BGI, ECO:0007744|PDB:2BGJ}
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) IN COMPLEX WITH FAD, FUNCTION,
RP CATALYTIC ACTIVITY, AND COFACTOR.
RC STRAIN=DSM 938 / 37b4;
RX PubMed=16128574; DOI=10.1021/bi0508183;
RA Nogues I., Perez-Dorado I., Frago S., Bittel C., Mayhew S.G.,
RA Gomez-Moreno C., Hermoso J.A., Medina M., Cortez N., Carrillo N.;
RT "The ferredoxin-NADP(H) reductase from Rhodobacter capsulatus: molecular
RT structure and catalytic mechanism.";
RL Biochemistry 44:11730-11740(2005).
RN [3] {ECO:0007744|PDB:2VNH, ECO:0007744|PDB:2VNI, ECO:0007744|PDB:2VNJ, ECO:0007744|PDB:2VNK}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH FAD AND NADP, AND
RP COFACTOR.
RX PubMed=18973834; DOI=10.1016/j.bbapap.2008.09.013;
RA Bortolotti A., Perez-Dorado I., Goni G., Medina M., Hermoso J.A.,
RA Carrillo N., Cortez N.;
RT "Coenzyme binding and hydride transfer in Rhodobacter capsulatus
RT ferredoxin/flavodoxin NADP(H) oxidoreductase.";
RL Biochim. Biophys. Acta 1794:199-210(2009).
RN [4] {ECO:0007744|PDB:4K1X}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 14-264 IN COMPLEX WITH FAD,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ALA-264.
RX PubMed=24016470; DOI=10.1016/j.bbabio.2013.08.008;
RA Bortolotti A., Sanchez-Azqueta A., Maya C.M., Velazquez-Campoy A.,
RA Hermoso J.A., Medina M., Cortez N.;
RT "The C-terminal extension of bacterial flavodoxin-reductases: involvement
RT in the hydride transfer mechanism from the coenzyme.";
RL Biochim. Biophys. Acta 1837:33-43(2014).
CC -!- FUNCTION: Transports electrons between flavodoxin or ferredoxin and
CC NADPH. {ECO:0000269|PubMed:14572660, ECO:0000269|PubMed:16128574,
CC ECO:0000269|PubMed:24016470}.
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:14572660, ECO:0000269|PubMed:24016470};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + reduced [flavodoxin] = 2 H(+) + NADPH + oxidized
CC [flavodoxin]; Xref=Rhea:RHEA:50756, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC COMP:10623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.19.1.1;
CC Evidence={ECO:0000269|PubMed:14572660, ECO:0000269|PubMed:16128574,
CC ECO:0000269|PubMed:24016470};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:14572660, ECO:0000269|PubMed:16128574,
CC ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=93 uM for NADPH (in the presence of K(3)Fe(CN)(6))
CC {ECO:0000269|PubMed:24016470};
CC KM=85 uM for NADPH (in the presence of 2,6-dichlorophenolindophenol)
CC {ECO:0000269|PubMed:24016470};
CC Note=kcat is 222 sec(-1) with K(3)Fe(CN)(6) as substrate. kcat is 20
CC sec(-1) with 2,6-dichlorophenolindophenol as substrate.
CC {ECO:0000269|PubMed:24016470};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14572660}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:14572660}.
CC -!- INDUCTION: Induced under oxidative stress conditions.
CC {ECO:0000269|PubMed:14572660}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF35905.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF232063; AAF35905.1; ALT_INIT; Genomic_DNA.
DR PDB; 2BGI; X-ray; 1.68 A; A=1-270.
DR PDB; 2BGJ; X-ray; 2.10 A; A/B/C/D=1-270.
DR PDB; 2VNH; X-ray; 2.27 A; A=1-270.
DR PDB; 2VNI; X-ray; 2.24 A; A=1-270.
DR PDB; 2VNJ; X-ray; 2.13 A; A=1-270.
DR PDB; 2VNK; X-ray; 1.93 A; A/B/C/D=1-270.
DR PDB; 4K1X; X-ray; 1.70 A; A/B=14-264.
DR PDBsum; 2BGI; -.
DR PDBsum; 2BGJ; -.
DR PDBsum; 2VNH; -.
DR PDBsum; 2VNI; -.
DR PDBsum; 2VNJ; -.
DR PDBsum; 2VNK; -.
DR PDBsum; 4K1X; -.
DR AlphaFoldDB; Q9L6V3; -.
DR SMR; Q9L6V3; -.
DR DrugBank; DB04450; Heptyl 1-Thiohexopyranoside.
DR BRENDA; 1.18.1.2; 5381.
DR BRENDA; 1.19.1.1; 5381.
DR EvolutionaryTrace; Q9L6V3; -.
DR GO; GO:0005737; C:cytoplasm; 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 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; Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW NADP; Nucleotide-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:14572660"
FT CHAIN 2..270
FT /note="Flavodoxin/ferredoxin--NADP reductase"
FT /id="PRO_0000441750"
FT DOMAIN 12..113
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 62..65
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16128574,
FT ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470"
FT BINDING 78..80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16128574,
FT ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470"
FT BINDING 86..88
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16128574,
FT ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470"
FT BINDING 126
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18973834"
FT BINDING 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16128574,
FT ECO:0000269|PubMed:18973834, ECO:0000269|PubMed:24016470"
FT BINDING 156
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18973834"
FT BINDING 192..193
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18973834"
FT BINDING 201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18973834"
FT BINDING 238
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18973834"
FT BINDING 264..270
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:16128574,
FT ECO:0000269|PubMed:18973834"
FT MUTAGEN 264
FT /note="A->Y: 3-fold decrease in kcat."
FT /evidence="ECO:0000269|PubMed:24016470"
FT STRAND 15..26
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 162..173
FT /evidence="ECO:0007829|PDB:2BGI"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:2BGI"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 202..207
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:2BGI"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:2BGI"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:2BGI"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:2BGI"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:2BGI"
FT TURN 252..254
FT /evidence="ECO:0007829|PDB:4K1X"
FT STRAND 257..268
FT /evidence="ECO:0007829|PDB:2BGI"
SQ SEQUENCE 270 AA; 30233 MW; 12DE6B7A75D03D10 CRC64;
MNETTPIAPA KVLPDAQTVT SVRHWTDTLF SFRVTRPQTL RFRSGEFVMI GLLDDNGKPI
MRAYSIASPA WDEELEFYSI KVPDGPLTSR LQHIKVGEQI ILRPKPVGTL VIDALLPGKR
LWFLATGTGI APFASLMREP EAYEKFDEVI MMHACRTVAE LEYGRQLVEA LQEDPLIGEL
VEGKLKYYPT TTREEFHHMG RITDNLASGK VFEDLGIAPM NPETDRAMVC GSLAFNVDVM
KVLESYGLRE GANSEPREFV VEKAFVGEGI
