ID E5RDD5_CUCME Unreviewed; 360 AA.
AC E5RDD5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Ferredoxin--NADP reductase, chloroplastic {ECO:0000256|PIRNR:PIRNR000361};
DE Short=FNR {ECO:0000256|PIRNR:PIRNR000361};
DE EC=1.18.1.2 {ECO:0000256|PIRNR:PIRNR000361};
OS Cucumis melo subsp. melo.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=412675 {ECO:0000313|EMBL:ADN33943.1};
RN [1] {ECO:0000313|EMBL:ADN33943.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Young leaves {ECO:0000313|EMBL:ADN33943.1};
RX PubMed=20509895; DOI=10.1186/1471-2164-11-339;
RA Gonzalez V.M., Garcia-Mas J., Arus P., Puigdomenech P.;
RT "Generation of a BAC-based physical map of the melon genome.";
RL BMC Genomics 11:339-339(2010).
RN [2] {ECO:0000313|EMBL:ADN33943.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Young leaves {ECO:0000313|EMBL:ADN33943.1};
RX PubMed=21073723; DOI=10.1186/1471-2229-10-246;
RA Gonzalez V.M., Benjak A., Henaff E.M., Mir G., Casacuberta J.M.,
RA Garcia-Mas J., Puigdomenech P.;
RT "Sequencing of 6.7 Mb of the melon genome using a BAC pooling strategy.";
RL BMC Plant Biol. 10:246-246(2010).
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 Evidence={ECO:0000256|ARBA:ARBA00001005,
CC ECO:0000256|PIRNR:PIRNR000361};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- PATHWAY: Energy metabolism; photosynthesis.
CC {ECO:0000256|ARBA:ARBA00004748}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000256|ARBA:ARBA00004470}. Plastid, chloroplast thylakoid
CC membrane {ECO:0000256|ARBA:ARBA00004185}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004185}; Stromal side
CC {ECO:0000256|ARBA:ARBA00004185}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312, ECO:0000256|PIRNR:PIRNR000361}.
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DR EMBL; HM854776; ADN33943.1; -; Genomic_DNA.
DR AlphaFoldDB; E5RDD5; -.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast 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 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; 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; -; 1.
DR PANTHER; PTHR43314:SF27; FERREDOXIN--NADP REDUCTASE, LEAF ISOZYME 2, CHLOROPLASTIC; 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; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000361};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000361};
KW NADP {ECO:0000256|PIRNR:PIRNR000361, ECO:0000256|PIRSR:PIRSR000361-1};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000361};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 81..203
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 142
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 162
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 250..251
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 280..281
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 290
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 319..320
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ SEQUENCE 360 AA; 40482 MW; 36F350B2E17F0C99 CRC64;
MAAAVTAAAV SFPSKSSSLP SRTPLISPDR IFLKKVPVFY HGGRVAVSPI RAQVTTEAPA
KVEKESKKQE EGIVVNKFKP KTPYIGRCLL NTKITGDDAP GETWHMVFST EGEVPYKEGQ
SIGVIADGED KNGKPHKLRL YSIASSALGD FGDSKTVSLC VKRLVYTNEQ GEIVKGVCSN
FLCDLKPGAE VKITGPVGKE MLMPKDPNAT VIMLATGTGI APFRSFLWKM FFEKHEDYKF
NGLAWLFLGV PTSSSLLYKE EFEKMKEKYP ENFRLDFAVS REQTNEKGEK MYIQTRMAEY
AEELWELLKK DNTFVYMCGL KGMEKGIDDI MDSLAARDGI DWQEYKRQLK RSEQWNVEVY
//
