ID Q47AY5_DECAR Unreviewed; 270 AA.
AC Q47AY5;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Flavodoxin/ferredoxin--NADP reductase {ECO:0000256|ARBA:ARBA00020327};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.19.1.1 {ECO:0000256|ARBA:ARBA00012872};
DE AltName: Full=Ferredoxin (flavodoxin):NADP(+) oxidoreductase {ECO:0000256|ARBA:ARBA00030173};
DE AltName: Full=Ferredoxin--NADP reductase {ECO:0000256|ARBA:ARBA00029856};
DE AltName: Full=Flavodoxin--NADP reductase {ECO:0000256|ARBA:ARBA00030000};
GN OrderedLocusNames=Daro_3266 {ECO:0000313|EMBL:AAZ47996.1};
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087 {ECO:0000313|EMBL:AAZ47996.1};
RN [1] {ECO:0000313|EMBL:AAZ47996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RCB {ECO:0000313|EMBL:AAZ47996.1};
RA Salinero K.K., Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Trong S.,
RA Schmutz J., Larimer F., Land M., Ivanova N., Richardson P.;
RT "Complete sequence of Dechloromonas aromatica RCB.";
RL Submitted (AUG-2005) 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;
CC Evidence={ECO:0000256|ARBA:ARBA00001005};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + reduced [flavodoxin] = 2 H(+) + NADPH + oxidized
CC [flavodoxin]; Xref=Rhea:RHEA:50756, Rhea:RHEA-COMP:10622, Rhea:RHEA-
CC COMP:10623, ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58210, ChEBI:CHEBI:58349; EC=1.19.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000579};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ferredoxin--NADP reductase type 1 family.
CC {ECO:0000256|ARBA:ARBA00008312}.
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DR EMBL; CP000089; AAZ47996.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47AY5; -.
DR STRING; 159087.Daro_3266; -.
DR KEGG; dar:Daro_3266; -.
DR eggNOG; COG1018; Bacteria.
DR HOGENOM; CLU_003827_3_0_4; -.
DR OrthoDB; 9784483at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004324; F:ferredoxin-NADP+ reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd06195; FNR1; 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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR033892; FNR_bac.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47878:SF2; FLAVODOXIN_FERREDOXIN--NADP REDUCTASE; 1.
DR PANTHER; PTHR47878; OXIDOREDUCTASE FAD/NAD(P)-BINDING DOMAIN PROTEIN; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 18..119
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 270 AA; 30328 MW; 08557B7B23C9AB58 CRC64;
MLTPASTFRR GPLPAPTDKA TAERILDIRR WTDKLISVRT TRNVSFRFQP GQFARIGIAS
DSGGTIWRPY SMVSANYDEH LEFFSIIVPN GAFSTKLALA SVGDTLYVEK QPYGYLTTSR
FVGGQDLWML ATGTGIAPFL SILRDPEVWA QYDNLLLAYS VRHISELAYR NEIASIAQEE
PFAEHGHKLR FAPIVTREAV PGMLNRRLTD LLHDGELEKS IGLPIDAERA RMLICGNPQM
LDDVRQVLTA RGFRPDLGRA PGHFACENYW
//
