ID A0A929A9Q3_9CYAN Unreviewed; 404 AA.
AC A0A929A9Q3;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
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 ORFNames=IQ267_22345 {ECO:0000313|EMBL:MBE9102184.1};
OS filamentous cyanobacterium LEGE 07170.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales.
OX NCBI_TaxID=1828880 {ECO:0000313|EMBL:MBE9102184.1, ECO:0000313|Proteomes:UP000627638};
RN [1] {ECO:0000313|EMBL:MBE9102184.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=LEGE 07170 {ECO:0000313|EMBL:MBE9102184.1};
RA Castelo-Branco R., Eusebio N., Adriana R., Vieira A.,
RA Brugerolle De Fraissinette N., Rezende De Castro R., Schneider M.P.,
RA Vasconcelos V., Leao P.N.;
RL Submitted (OCT-2020) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00047776,
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}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312, ECO:0000256|PIRNR:PIRNR000361}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBE9102184.1}.
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DR EMBL; JADEXA010000056; MBE9102184.1; -; Genomic_DNA.
DR Proteomes; UP000627638; Unassembled WGS sequence.
DR GO; GO:0030089; C:phycobilisome; IEA:UniProtKB-UniRule.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06208; CYPOR_like_FNR; 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 {ECO:0000256|ARBA:ARBA00022549};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000361};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000361}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000361};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000361};
KW Phycobilisome {ECO:0000256|ARBA:ARBA00022738, ECO:0000256|PROSITE-
KW ProRule:PRU00771}; Reference proteome {ECO:0000313|Proteomes:UP000627638};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 17..74
FT /note="CpcD-like"
FT /evidence="ECO:0000259|PROSITE:PS51441"
FT DOMAIN 121..245
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 72..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..98
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 183
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 203
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 260
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 326..327
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 365..366
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 402
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ SEQUENCE 404 AA; 45030 MW; 8852C24E25E69C40 CRC64;
MFSQSAMGGF TNSISNSRLF VYEVEGIRQV GADSIGSPIR RSGSTFITVP YSRMNEEMKR
ISRMGGKILS IRPINGETNG QGSSTTSSAP SQAASQSQEK SMTQAAKKKK SDVPVNLYRP
KDPFIGKCIS NEPLVGEGGN GIVQHITFDL SGGDLHYLEG QSIGIIPEGT DDKGKPHKLR
LYSIASTRHG DNMDDKTVSL CVRQLEYKHP ESGETVYGVC STYLCNLEPG ADVKITGPVG
KEMLLPDDPD AKIVMMATGT GIAPFRAYLW RMFKDDEKAA NPDYEFKGFA WLIFGIPKTP
NILYKEELEE LQSKYPDNFR MTYAISREQQ NSEGGRMYIQ HRVAEHADEI WNMVKDEKTH
VYICGLKGME DGIDAAMSAA AEKEGVNWKE YQRSIKERWH VETY
//
