ID FENR2_TOBAC Reviewed; 375 AA. AC O04397; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 16-JUN-2009, entry version 68. DE RecName: Full=Ferredoxin--NADP reductase, root-type isozyme, chloroplastic; DE Short=FNR; DE EC=1.18.1.2; DE Flags: Precursor; OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae; OC Nicotiana. OX NCBI_TaxID=4097; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=cv. Bright Yellow 2; RA Kumada H.O., Aoki H., Doyama N., Ida S.; RT "Nucleotide sequence of a ferredoxin-NADP+ oxidoreductase cDNA from RT cultured tobacco cells."; RL (er) Plant Gene Register PGR98-038. CC -!- FUNCTION: May play a key role in regulating the relative amounts CC of cyclic and non-cyclic electron flow to meet the demands of the CC plant for ATP and reducing power. Is involved in nitrate CC assimilation. CC -!- CATALYTIC ACTIVITY: 2 reduced ferredoxin + NADP(+) + H(+) = 2 CC oxidized ferredoxin + NADPH. CC -!- COFACTOR: FAD. CC -!- PATHWAY: Energy metabolism; photosynthesis. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity). CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 CC family. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AB004307; BAA20365.1; -; mRNA. DR PIR; T02215; T02215. DR HSSP; Q41736; 1JB9. DR SMR; O04397; 66-375. DR BRENDA; 1.18.1.2; 298. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0042651; C:thylakoid membrane; IEA:InterPro. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0050660; F:FAD binding; IEA:InterPro. DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:EC. DR GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase. DR InterPro; IPR012146; Frd-NADP+_RD. DR InterPro; IPR015701; FRD_Red. DR InterPro; IPR001433; OxRdtase_FAD/NAD_bd. DR PANTHER; PTHR19384:SF1; FRD_Red; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF000361; Frd-NADP+_RD; 1. DR PRINTS; PR00371; FPNCR. DR PROSITE; PS51384; FAD_FR; 1. PE 2: Evidence at transcript level; KW Chloroplast; Electron transport; FAD; Flavoprotein; NADP; KW Oxidoreductase; Photosynthesis; Plastid; Transit peptide; Transport. FT TRANSIT 1 60 Chloroplast (Potential). FT CHAIN 61 375 Ferredoxin--NADP reductase, root-type FT isozyme, chloroplastic. FT /FTId=PRO_0000019416. FT DOMAIN 91 219 FAD-binding FR-type. FT NP_BIND 151 154 FAD (By similarity). FT NP_BIND 172 174 FAD (By similarity). FT NP_BIND 193 195 FAD (By similarity). FT NP_BIND 266 267 NADP (By similarity). FT NP_BIND 296 297 NADP (By similarity). FT NP_BIND 334 335 NADP (By similarity). FT BINDING 174 174 NADP (By similarity). FT BINDING 178 178 FAD (By similarity). FT BINDING 235 235 FAD (By similarity). FT BINDING 235 235 NADP; via amide nitrogen (By similarity). FT BINDING 306 306 NADP (By similarity). FT BINDING 373 373 NADP (By similarity). SQ SEQUENCE 375 AA; 41958 MW; AB5ED3988F746B92 CRC64; MAHSALSQVS VAVPLQTDSS FRRSTFKATS ITFSDRSSWI SMPPIDLKAA PSRNQHIVCM SVQQASKAKV SVSPLSLEDA KEPPLNIYKP KEPYTATIVS VERLVGPKAP GETCHIVIDH DGNLPYWEGQ SYGVIPPGEN PKKPGNPHNV RLYLIASTRY GDSFDGKTAS LCVRRAVYYD PETGKEDPSK NGVCSNFLCD SKPGDKVKIT GPSGKIMLLP EEIPNATHIM IGTGTGVAPF RGYLRRMFME SVPTKFNGLA WLFLGVANTD SLLYDDEFTK YLNDYPGNFR YDRALSREQK NNKGGKMYVQ DKIEEYSDEI FKLLDEGAHI YFCGLKGMMP GIQDTLKRVA ERRGESWEQK LSQLKKNKQW HVEVY //