ID E4TBR4_RIEAD Unreviewed; 350 AA.
AC E4TBR4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Ferredoxin--NADP reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE Short=FNR {ECO:0000256|HAMAP-Rule:MF_01685};
DE Short=Fd-NADP(+) reductase {ECO:0000256|HAMAP-Rule:MF_01685};
DE EC=1.18.1.2 {ECO:0000256|HAMAP-Rule:MF_01685};
GN ORFNames=RA0C_1037 {ECO:0000313|EMBL:AFD55966.1};
OS Riemerella anatipestifer (strain ATCC 11845 / DSM 15868 / JCM 9532 / NCTC
OS 11014).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=693978 {ECO:0000313|EMBL:AFD55966.1, ECO:0000313|Proteomes:UP000010093};
RN [1] {ECO:0000313|EMBL:AFD55966.1, ECO:0000313|Proteomes:UP000010093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15868 {ECO:0000313|Proteomes:UP000010093};
RX PubMed=22628503; DOI=10.1128/JB.00366-12;
RA Wang X., Zhu D., Wang M., Cheng A., Jia R., Zhou Y., Chen Z., Luo Q.,
RA Liu F., Wang Y., Chen X.Y.;
RT "Complete genome sequence of Riemerella anatipestifer reference strain.";
RL J. Bacteriol. 194:3270-3271(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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01685};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01685};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01685};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01685}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 2 family.
CC {ECO:0000256|HAMAP-Rule:MF_01685}.
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DR EMBL; CP003388; AFD55966.1; -; Genomic_DNA.
DR RefSeq; WP_013446920.1; NC_017045.1.
DR AlphaFoldDB; E4TBR4; -.
DR KEGG; rai:RA0C_1037; -.
DR KEGG; ran:Riean_0798; -.
DR PATRIC; fig|693978.17.peg.1041; -.
DR HOGENOM; CLU_031864_5_5_10; -.
DR Proteomes; UP000010093; 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; FAD/NAD(P)-binding domain; 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 PANTHER; PTHR48105:SF15; FERREDOXIN--NADP REDUCTASE; 1.
DR PANTHER; PTHR48105; THIOREDOXIN REDUCTASE 1-RELATED-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|HAMAP-Rule:MF_01685};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01685};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01685};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01685}.
FT DOMAIN 5..291
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT BINDING 14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 41
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 121
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
FT BINDING 327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01685"
SQ SEQUENCE 350 AA; 38674 MW; 0796C17A346F900D CRC64;
MITTDLLIIG AGPTGLFAVF EAGLLKLKCH IIDALPQPGG QLAELYPKKP IFDIPGYPSV
NAGELVDNLM EQIKQFQPGF TLAETAVSLE KIDDEWFEVI TNKGTVHRAK AVAIAGGLGT
FEPRKPLLEN LEKYEENGVE YFVKDPEVFR DKKIVIAGGG DSALDWSIFL SNVAKEVTLV
HRRNEFRGAL DSVEKVQELK NQGKINLVTP AEVVELKGSN TLESIVIERE GEKTEIETDY
FIPLFGLTPK LGPIADWGLE IEKNSIKVNN ALDYQTNREG IYAIGDINTY PGKLKLILCG
FHEATLMCQS VYNRLNPGKK YVLKYTTVSG VDGFDGSRKE AEKAVVKKID
//
