FENR_RHOPA
ID FENR_RHOPA Reviewed; 342 AA.
AC Q6N2U4;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ferredoxin--NADP reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=FNR {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=Fd-NADP(+) reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE EC=1.18.1.2 {ECO:0000255|HAMAP-Rule:MF_01685};
GN OrderedLocusNames=RPA3954;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01685};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01685};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01685};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01685}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01685}.
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DR EMBL; BX572605; CAE29395.1; -; Genomic_DNA.
DR RefSeq; WP_011159490.1; NC_005296.1.
DR PDB; 5YGQ; X-ray; 2.40 A; A/B=1-342.
DR PDBsum; 5YGQ; -.
DR AlphaFoldDB; Q6N2U4; -.
DR SMR; Q6N2U4; -.
DR STRING; 258594.RPA3954; -.
DR PRIDE; Q6N2U4; -.
DR EnsemblBacteria; CAE29395; CAE29395; RPA3954.
DR GeneID; 66895069; -.
DR KEGG; rpa:RPA3954; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_5; -.
DR OMA; PEKVIYD; -.
DR PhylomeDB; Q6N2U4; -.
DR BioCyc; RPAL258594:TX73_RS20180-MON; -.
DR Proteomes; UP000001426; Chromosome.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01685; FENR2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR022890; Fd--NADP_Rdtase_type_2.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..342
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000364913"
FT BINDING 17
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 44
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 89
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 289
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 330
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:5YGQ"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 43..48
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:5YGQ"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:5YGQ"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 164..173
FT /evidence="ECO:0007829|PDB:5YGQ"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 178..187
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 209..219
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 256..260
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5YGQ"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:5YGQ"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 300..318
FT /evidence="ECO:0007829|PDB:5YGQ"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:5YGQ"
FT HELIX 333..339
FT /evidence="ECO:0007829|PDB:5YGQ"
SQ SEQUENCE 342 AA; 37017 MW; 744CDF19FB76121A CRC64;
MTETIKTDVL IVGAGPCGLF AVFELGLLDV KAHLVDILDK VGGQCAELYP EKPIYDIPGI
PMVTGHGLTE ALMEQIKPFN PTFHLSEMVE NVEKIGDPGF RVTTNAGKVF ECTVLVVAAG
GGSFLPKRPP VPGVEAYEGT SVHYAVRKME DFRGKDILIV GGGDSALDWT LNLNPIAKSM
TLVHRRDDFR GAPHSVEQMR QLVASGKLDL KIGQITELQG DNGQLTGATV KLNDNTTSQI
KCDAMLPFFG LTMKLGPVAN WGLDLENNLI PVDTGTFETN VPGIFAIGDI NTYPGKLKLI
LSGFHEGALM AQKAVKYVYP DKRVVFQYTT SSTNLQKKLG VN
