ID L2F790_9GAMM Unreviewed; 264 AA.
AC L2F790;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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 ORFNames=MOMA_00110 {ECO:0000313|EMBL:ELA08770.1};
OS Moraxella macacae 0408225.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=1230338 {ECO:0000313|EMBL:ELA08770.1, ECO:0000313|Proteomes:UP000023795};
RN [1] {ECO:0000313|EMBL:ELA08770.1, ECO:0000313|Proteomes:UP000023795}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0408225 {ECO:0000313|EMBL:ELA08770.1,
RC ECO:0000313|Proteomes:UP000023795};
RX PubMed=23409273;
RA Ladner J.T., Whitehouse C.A., Koroleva G.I., Palacios G.F.;
RT "Genome Sequence of Moraxella macacae 0408225, a Novel Bacterial Species
RT Isolated from a Cynomolgus Macaque with Epistaxis.";
RL Genome Announc. 1:E00188-12(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELA08770.1}.
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DR EMBL; ANIN01000001; ELA08770.1; -; Genomic_DNA.
DR RefSeq; WP_009501141.1; NZ_ANIN01000001.1.
DR AlphaFoldDB; L2F790; -.
DR STRING; 1230338.MOMA_00110; -.
DR PATRIC; fig|1230338.3.peg.18; -.
DR eggNOG; COG1018; Bacteria.
DR OrthoDB; 9784483at2; -.
DR Proteomes; UP000023795; Unassembled WGS sequence.
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; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
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; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000023795}.
FT DOMAIN 3..114
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 264 AA; 30047 MW; 71794020BAD58E61 CRC64;
MTQTIKNVTV TDVKQWTKTL FSFKVVRPLE FKFTAGQFVR LGLNVNQIKR LNAQHDDTET
IFRAYSVVSS PYDEFIEFFS VVIPDGVFTS KLQYLQVGDT LQLDTTPYGF LTLSRYQAPA
PKDLWLLATG TGVAPFLSIL KTLDVWQTYQ KIYLIYSART QQELAYLEEI AQLQATYGEN
GADFQFIPIV TREADFDGLK QRLPTLILSG ELENCVKTNL NPKSSHVMLC GNPQMVDDTK
EALKQKGLTM NRRSEGNIAV ENYW
//
