ID U5NA47_9BURK Unreviewed; 258 AA.
AC U5NA47;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN ORFNames=Cenrod_2124 {ECO:0000313|EMBL:AGX88195.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX88195.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX88195.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX88195.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CP004885; AGX88195.1; -; Genomic_DNA.
DR RefSeq; WP_022775323.1; NC_022576.1.
DR AlphaFoldDB; U5NA47; -.
DR STRING; 946483.Cenrod_2124; -.
DR KEGG; cbx:Cenrod_2124; -.
DR PATRIC; fig|946483.4.peg.2140; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_3_0_4; -.
DR OrthoDB; 9784483at2; -.
DR Proteomes; UP000017184; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000017184}.
FT DOMAIN 2..103
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 258 AA; 29155 MW; D254F88CA99F8A90 CRC64;
MSAYLNETVL SVHHWTDRLF SFTTTRDVAL RFSNGHFTMI GLRMDGSKPL LRAYSIVSAN
YEDHLEFLSI KVPDGPLTSR LQHIQVGDHI VVGKKPTGTL LIDYLLPGKN LYLFGTGTGL
APFLSIVRDP ATYEKFETVV LVHGVRQVAE LAYHDYLTLE LPDHEFLGEM VSQQMRYYPT
VTRESFRNQG RITTLIDNGK LASDLHLPPI DPATDRAMIC GSPDFLQDLK KLLEKRGFLE
GNTTRPGDFV IERAFVEQ
//
