FENR_PELUB
ID FENR_PELUB Reviewed; 338 AA.
AC Q4FMZ1;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Ferredoxin--NADP reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=FNR {ECO:0000255|HAMAP-Rule:MF_01685};
DE Short=Fd-NADP(+) reductase {ECO:0000255|HAMAP-Rule:MF_01685};
DE EC=1.18.1.2 {ECO:0000255|HAMAP-Rule:MF_01685};
GN OrderedLocusNames=SAR11_0627;
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; Candidatus Pelagibacter.
OX NCBI_TaxID=335992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062;
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01685};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01685};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01685};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01685}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01685}.
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; CP000084; AAZ21448.1; -; Genomic_DNA.
DR RefSeq; WP_011281821.1; NC_007205.1.
DR AlphaFoldDB; Q4FMZ1; -.
DR SMR; Q4FMZ1; -.
DR STRING; 335992.SAR11_0627; -.
DR PRIDE; Q4FMZ1; -.
DR EnsemblBacteria; AAZ21448; AAZ21448; SAR11_0627.
DR GeneID; 66295133; -.
DR KEGG; pub:SAR11_0627; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_5_5; -.
DR OMA; PEKVIYD; -.
DR OrthoDB; 692968at2; -.
DR Proteomes; UP000002528; Chromosome.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR Gene3D; 3.50.50.60; -; 2.
DR HAMAP; MF_01685; FENR2; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR022890; Fd--NADP_Rdtase_type_2.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..338
FT /note="Ferredoxin--NADP reductase"
FT /id="PRO_0000364895"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 120
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT BINDING 325
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
SQ SEQUENCE 338 AA; 38034 MW; 06CAD4F4DDBF51C1 CRC64;
MIKTDALIIG AGPTGLFCAH QLGLIGLNCE IVDNLDKIGG QCIELYPDKP IYDIPAVPEC
TGEELTNNLI KQIKPFNIKF HLNERVEEVN KVNNKWIVKT NKKKEFVTPN IIIAGGVGSF
EPRKFSPKEC EKYENRSLFY SIKDKTIFQD KTISIFGGGD SALDWAIELS KSSYVNLIHR
RDEFTGAQLS IDKIKELEKS GKLKIYTKYQ LNSVKGEQNI KSIEIKHDDE SLKELETNYV
LGFFGLIMKL GPIVDWGLNL DKKTIPVNTE NFETNLNGIF AIGDICTYPG KLKLILSGFH
EGALAARGCF KYARPDEKLR FEFTTTSKAA QERLGVKK
