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FENR_ACIAC
ID   FENR_ACIAC              Reviewed;         358 AA.
AC   A1TRN6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 79.
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=Aave_3058;
OS   Acidovorax citrulli (strain AAC00-1) (Acidovorax avenae subsp. citrulli).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1.";
RL   Submitted (DEC-2006) 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; 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   -!- SEQUENCE CAUTION:
CC       Sequence=ABM33624.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000512; ABM33624.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041827504.1; NC_008752.1.
DR   AlphaFoldDB; A1TRN6; -.
DR   SMR; A1TRN6; -.
DR   STRING; 397945.Aave_3058; -.
DR   EnsemblBacteria; ABM33624; ABM33624; Aave_3058.
DR   KEGG; aav:Aave_3058; -.
DR   eggNOG; COG0492; Bacteria.
DR   HOGENOM; CLU_031864_5_5_4; -.
DR   OrthoDB; 692968at2; -.
DR   Proteomes; UP000002596; 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; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR022890; Fd--NADP_Rdtase_type_2.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..358
FT                   /note="Ferredoxin--NADP reductase"
FT                   /id="PRO_0000364780"
FT   BINDING         38
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         51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         91
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         126
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         301
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
FT   BINDING         341
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01685"
SQ   SEQUENCE   358 AA;  37297 MW;  D47D2A33408C4E83 CRC64;
     MENARLIEAD AVVIGAGPVG LFQVFQLGLQ GIAAHVVDAL PHVGGQCAEL YADKPIYDIP
     GVPVCTGREL VALLNRQIAP FSPQLHLSQR VETLQPAPDG GFLFATDAGA ALHARTVFIA
     AGVGAFVPRT LKIDGIERFH GTQVFHHEEP APTRGRQVVV LGGEDTAVAR AIACAEPGPE
     AAASVTLVHR RDAFQAAPQD LARLQALRDS GRIRVLAAQV TGIEAAAQAG TPEPGRLTGV
     RLLASDGTEQ GLPLDTLLLC LGVSPRLGPV ADWGLALERK QVKVDTATFS AGVPGLYAVG
     DINTYPGKRK LILCGFHEAT LAAFAAAEHL AGSPVALQYT TTSTRLKERL GVAGAGTP
 
 
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