FENR_CYAPA
ID FENR_CYAPA Reviewed; 363 AA.
AC Q00598;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ferredoxin--NADP reductase, cyanelle;
DE Short=FNR;
DE EC=1.18.1.2;
DE Flags: Precursor;
GN Name=PETH;
OS Cyanophora paradoxa.
OC Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX NCBI_TaxID=2762;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 66-90.
RC STRAIN=UTEX LB 555 / Pringsheim;
RX PubMed=8490125; DOI=10.1007/bf00023600;
RA Jakowitsch J., Bayer M.G., Maier T.L., Luettke A., Gebhart U.B.,
RA Brandtner M., Hamilton B., Neumann-Spallart C., Michalowski C.B.,
RA Bohnert H.J., Schenk H.E.A., Loeffelhardt W.;
RT "Sequence analysis of pre-ferredoxin-NADP(+)-reductase cDNA from Cyanophora
RT paradoxa specifying a precursor for a nucleus-encoded cyanelle
RT polypeptide.";
RL Plant Mol. Biol. 21:1023-1033(1993).
CC -!- FUNCTION: May play a key role in regulating the relative amounts of
CC cyclic and non-cyclic electron flow to meet the demands of the plant
CC for ATP and reducing power.
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: Plastid, cyanelle stroma. Plastid, cyanelle
CC thylakoid membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Stromal side {ECO:0000305}. Note=In the vicinity of the
CC photosystem I. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000305}.
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DR EMBL; X66372; CAA47015.1; -; mRNA.
DR PIR; S33545; A56664.
DR AlphaFoldDB; Q00598; -.
DR SMR; Q00598; -.
DR GO; GO:0034060; C:cyanelle stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0033115; C:cyanelle thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; -; 1.
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; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF501178; FNR-PetH; 1.
DR PIRSF; PIRSF000361; Frd-NADP+_RD; 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 Cyanelle; Direct protein sequencing; Electron transport; FAD; Flavoprotein;
KW Membrane; NADP; Oxidoreductase; Photosynthesis; Plastid; Thylakoid;
KW Transit peptide; Transport.
FT TRANSIT 1..65
FT /note="Cyanelle"
FT /evidence="ECO:0000269|PubMed:8490125"
FT CHAIN 66..363
FT /note="Ferredoxin--NADP reductase, cyanelle"
FT /id="PRO_0000019418"
FT DOMAIN 84..206
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 142..145
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 163..165
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 180..182
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 253..254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 283..284
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 322..323
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 40491 MW; F5F5D1AEA91ADEBF CRC64;
MAFVASVPVF ANASGLKTEA KVCQKPALKN SFFRGEEVTS RSFFASQAVS AKPATTFEVD
TTIRAQAVDA KKKGDIPLNL FRPANPYIGK CIYNERIVGE GAPGETKHII FTHEGKVPYL
EGQSIGIIPP GTDKDGKPHK LRLYSIASTR HGDFGDDKTV SLSVKRLEYT DANGNLVKGV
CSNYLCDLKP GDEVMITGPV GTTMLMPEDQ SATIIMLATG TGIAPFRSFL RRMFEETHAD
YKFNGLAWLF LGVPTSSTLL YREELEKMQK ANPNNFRLDY AISREQTDSK GEKMYIQNRI
AEYANEFWNM IQKPNTFVYM CGLRGMEDGI QQCMEDIAKA NGTTWDAVVK GLKKEKRWHV
ETY
