ID Q31AF0_PROM9 Unreviewed; 370 AA.
AC Q31AF0;
DT 06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 06-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Ferredoxin--NADP reductase {ECO:0000256|ARBA:ARBA00013903, ECO:0000256|PIRNR:PIRNR000361};
DE Short=FNR {ECO:0000256|PIRNR:PIRNR000361};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223, ECO:0000256|PIRNR:PIRNR000361};
GN OrderedLocusNames=PMT9312_1086 {ECO:0000313|EMBL:ABB50145.1};
OS Prochlorococcus marinus (strain MIT 9312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales;
OC Prochlorococcaceae; Prochlorococcus.
OX NCBI_TaxID=74546 {ECO:0000313|EMBL:ABB50145.1, ECO:0000313|Proteomes:UP000002715};
RN [1] {ECO:0000313|Proteomes:UP000002715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9312 {ECO:0000313|Proteomes:UP000002715};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Thiel J., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Prochlorococcus marinus str. MIT 9312.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000256|ARBA:ARBA00004445}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004445}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004445}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312, ECO:0000256|PIRNR:PIRNR000361}.
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; CP000111; ABB50145.1; -; Genomic_DNA.
DR RefSeq; WP_011376636.1; NC_007577.1.
DR AlphaFoldDB; Q31AF0; -.
DR STRING; 74546.PMT9312_1086; -.
DR KEGG; pmi:PMT9312_1086; -.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_053066_0_0_3; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000002715; 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 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; IPR008333; Cbr1-like_FAD-bd_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; -; 1.
DR PANTHER; PTHR43314:SF27; FERREDOXIN--NADP REDUCTASE, LEAF ISOZYME 2, CHLOROPLASTIC; 1.
DR Pfam; PF00970; FAD_binding_6; 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 Antenna complex {ECO:0000256|ARBA:ARBA00022549};
KW FAD {ECO:0000256|PIRNR:PIRNR000361};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000361};
KW Membrane {ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|PIRNR:PIRNR000361, ECO:0000256|PIRSR:PIRSR000361-1};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000361};
KW Phycobilisome {ECO:0000256|ARBA:ARBA00022738};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..210
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 35..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 150
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 170
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 225
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 290..291
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 329..330
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 368
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ SEQUENCE 370 AA; 41633 MW; 36D474C306CC16C4 CRC64;
MYSQSTVIAG GLAHIPVVIG VFYFILKTFS KRASNFPQDT EPKKSQVKSV EQKSVPKPAP
VAKGVTNNVV KKKKHADVPV NIYRPKTPYE GTVIENYSLL KEGAIGRVNH ITFDLKDSDP
FLNYVEGQSI GIMPAGEDAN GKPHKLRLYS IASTRHGDDY KGNTVSLCVR QLQYEKDGET
INGVCSTYLC DIKPGDKVKI TGPVGKEMLL PDEEDANIVM LATGTGIAPM RAYLRRMFEA
TEKEKNKWNF KGKAWLFMGA PKSANLLYEE DLQRYLTDYP DNFTYTKAIS REQQNTKGGR
MYIQDRVLES ANELFNMIED EKTHIYLCGL KGMEPGIDEA MTKAAEEKGL NWSELRPQLK
KAGRWHVETY
//
