ID A0A1G5A988_9BURK Unreviewed; 257 AA.
AC A0A1G5A988;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=SAMN03159363_6181 {ECO:0000313|EMBL:SCX74437.1};
OS Variovorax sp. EL159.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1566270 {ECO:0000313|EMBL:SCX74437.1, ECO:0000313|Proteomes:UP000199507};
RN [1] {ECO:0000313|EMBL:SCX74437.1, ECO:0000313|Proteomes:UP000199507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL159 {ECO:0000313|EMBL:SCX74437.1,
RC ECO:0000313|Proteomes:UP000199507};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FMUJ01000010; SCX74437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5A988; -.
DR STRING; 1566270.SAMN03159363_6181; -.
DR OrthoDB; 9784483at2; -.
DR Proteomes; UP000199507; Unassembled WGS sequence.
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:SF1; 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 4: Predicted;
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 2..102
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 257 AA; 29181 MW; F2C0C9E375370309 CRC64;
MSAFSEERVL SVHHWTDRLF TFTTTRDAAL RFSNGHFTMI GLKVNNKPLL RAYSIVSPNY
EEHLEFLSIK VEDGPLTSKL QHIQVGDTII VGRKPTGTLL IDYTLPAKRL YLFGTGTGLA
PFMSIIRDPD TYEKFEQVIL VHGVRQVDEL AYHDLVTDHL PKHEILGEMI EKQLLYYPTV
TREEFRNQGR ITDLIESNKL TDDLGLPPLN VEEDRVMLCG SPGLLVDLKH ILEARGFKEG
NTSTPGDFVV ERAFAEK
//
