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 02-SEP-2026, entry version 147. 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; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales; OC 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=2 reduced [2Fe-2S]-[ferredoxin] + NADP(+) + H(+) = 2 oxidized CC [2Fe-2S]-[ferredoxin] + NADPH; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000019; BAB75820.1; -; Genomic_DNA. DR PIR; AB2321; AB2321. DR RefSeq; WP_010998260.1; NC_003272.1. DR AlphaFoldDB; P58558; -. DR SMR; P58558; -. DR STRING; 103690.gene:10496169; -. DR DrugBank; DB03147; Flavin adenine dinucleotide. DR DrugBank; DB03461; Nicotinamide adenine dinucleotide phosphate. DR KEGG; ana:all4121; -. DR eggNOG; COG0369; Bacteria. DR OrthoDB; 9789468at2; -. DR Proteomes; UP000002483; Chromosome. DR GO; GO:0030089; C:phycobilisome; IEA:InterPro. 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 CDD; cd06208; CYPOR_like_FNR; 1. DR FunFam; 2.40.30.10:FF:000199; Ferredoxin--NADP reductase; 1. DR FunFam; 3.40.50.80:FF:000008; Ferredoxin--NADP reductase, chloroplastic; 1. DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1. DR Gene3D; 2.40.30.10; Translation factors; 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 NCBIfam; NF045929; FNRPetHCyano; 1. DR PANTHER; 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; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1. DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 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..133 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 //