ID K7VXT5_9NOST Unreviewed; 463 AA.
AC K7VXT5;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
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=ANA_C12305 {ECO:0000313|EMBL:AFW95040.1};
OS Anabaena sp. 90.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=46234 {ECO:0000313|EMBL:AFW95040.1, ECO:0000313|Proteomes:UP000010101};
RN [1] {ECO:0000313|EMBL:AFW95040.1, ECO:0000313|Proteomes:UP000010101}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=90 {ECO:0000313|EMBL:AFW95040.1};
RX PubMed=23148582; DOI=10.1186/1471-2164-13-613;
RA Wang H., Sivonen K., Rouhiainen L., Fewer D.P., Lyra C., Rantala-Ylinen A.,
RA Vestola J., Jokela J., Rantasarkka K., Li Z., Liu B.;
RT "Genome-derived insights into the biology of the hepatotoxic bloom-forming
RT cyanobacterium Anabaena sp. strain 90.";
RL BMC Genomics 13:613-613(2012).
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}.
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DR EMBL; CP003284; AFW95040.1; -; Genomic_DNA.
DR RefSeq; WP_015080197.1; NC_019427.1.
DR AlphaFoldDB; K7VXT5; -.
DR STRING; 46234.ANA_C12305; -.
DR KEGG; anb:ANA_C12305; -.
DR PATRIC; fig|46234.3.peg.2605; -.
DR eggNOG; COG0369; Bacteria.
DR HOGENOM; CLU_053066_0_0_3; -.
DR OrthoDB; 9789468at2; -.
DR Proteomes; UP000010101; Chromosome chANA01.
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: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; 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 PANTHER; PTHR43314; -; 1.
DR PANTHER; PTHR43314:SF27; FERREDOXIN--NADP REDUCTASE, LEAF ISOZYME 2, CHLOROPLASTIC; 1.
DR Pfam; PF01383; CpcD; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF501178; FNR-PetH; 2.
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|PIRNR:PIRNR000361};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000361};
KW NADP {ECO:0000256|PIRNR:PIRNR000361, ECO:0000256|PIRSR:PIRSR000361-1};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000361,
KW ECO:0000313|EMBL:AFW95040.1};
KW Phycobilisome {ECO:0000256|ARBA:ARBA00022738, ECO:0000256|PROSITE-
KW ProRule:PRU00771}; Reference proteome {ECO:0000313|Proteomes:UP000010101};
KW Thylakoid {ECO:0000256|ARBA:ARBA00023078}.
FT DOMAIN 17..75
FT /note="CpcD-like"
FT /evidence="ECO:0000259|PROSITE:PS51441"
FT DOMAIN 178..302
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 124..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 240
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 317
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 353..354
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 383..384
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 422..423
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
FT BINDING 461
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000361-1"
SQ SEQUENCE 463 AA; 51539 MW; 371D1D959C2DD7DE CRC64;
MYNQGAVEGA ANIESGSRVF VYEVMGLRQT EETDQTNYPI RKSGSVFIRV PYNRMNQEMR
RITRLGGKIV SIQPVTALEQ VNGKVELVAA EITVSRDSQP VNEIVELATA DIPVSTEVKA
EVNANEEEHG KATPVSNASE AKGFAKSPAK EKKGQTMTQA KAKKDAHADV PVNIYRPNAP
FIGKCISNET LVKEGGIGIV QHLKFDLSAG NLRYLEGQSI GIIPPGVDKN GKPEKLRLYS
IASTRHGDNL DDKTISLCVR QLEYKHPETG ETVYGVCSTY LTKIKPGDDV KITGPVGKEM
LLPEDPEANV IMLATGTGIA PMRTYLWRMF KDAERKANPE YQFKGFSWLL FGVPTSPNIL
YKEELEAMQE KYPKNFRLTY AISREQNNPA GGRMYIQDRV AEHADELWQL IKNEKTHTYI
CGLRGMEDGI DAALSAAAAK EGVVWSDYQK NLKKAHRWHV ETY
//
