FENR_NOSS1
ID FENR_NOSS1 Reviewed; 440 AA.
AC P58558;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Ferredoxin--NADP reductase;
DE Short=FNR;
DE EC=1.18.1.2;
GN Name=petH; OrderedLocusNames=all4121;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Note=May be bound to the thylakoid membrane or anchored
CC to the thylakoid-bound phycobilisomes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; BA000019; BAB75820.1; -; Genomic_DNA.
DR PIR; AB2321; AB2321.
DR RefSeq; WP_010998260.1; NZ_RSCN01000010.1.
DR AlphaFoldDB; P58558; -.
DR SMR; P58558; -.
DR STRING; 103690.17133256; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate.
DR EnsemblBacteria; BAB75820; BAB75820; BAB75820.
DR KEGG; ana:all4121; -.
DR eggNOG; COG0369; Bacteria.
DR OMA; GKAWLFM; -.
DR OrthoDB; 707164at2; -.
DR Proteomes; UP000002483; Chromosome.
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; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW Antenna complex; FAD; Flavoprotein; Membrane; NADP; Oxidoreductase;
KW Phycobilisome; Reference proteome; Thylakoid.
FT CHAIN 1..440
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000167633"
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 98..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 /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 253..255
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 370..374
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 440 AA; 48838 MW; BB07AA1B99295C98 CRC64;
MSNQGAFDGA ANVESGSRVF VYEVVGMRQN EETDQTNYPI RKSGSVFIRV PYNRMNQEMQ
RITRLGGKIV SIQTVSALQQ LNGRTTIATV TDASSEIAKS EGNGKATPVK TDSGAKGFAK
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 EKTHTYICGL RGMEEGIDAA LSAAAAKEGV
TWSDYQKDLK KAGRWHVETY
