ID   A0A0Q6ZB08_9BRAD        Unreviewed;       257 AA.
AC   A0A0Q6ZB08;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   ORFNames=ASC80_11880 {ECO:0000313|EMBL:KQW20868.1};
OS   Afipia sp. Root123D2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW20868.1, ECO:0000313|Proteomes:UP000051348};
RN   [1] {ECO:0000313|EMBL:KQW20868.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20868.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW20868.1, ECO:0000313|Proteomes:UP000051348}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root123D2 {ECO:0000313|EMBL:KQW20868.1,
RC   ECO:0000313|Proteomes:UP000051348};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:KQW20868.1}.
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DR   EMBL; LMDP01000002; KQW20868.1; -; Genomic_DNA.
DR   RefSeq; WP_056297119.1; NZ_LMDP01000002.1.
DR   AlphaFoldDB; A0A0Q6ZB08; -.
DR   STRING; 1736436.ASC80_11880; -.
DR   OrthoDB; 9784483at2; -.
DR   Proteomes; UP000051348; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051348}.
FT   DOMAIN          2..102
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   257 AA;  28678 MW;  1E0F17DBE0AF5354 CRC64;
     MSAFHREKVL SVRHWTDSLF SFTATRNAGF RFQNGQFAMI GLEVEGRPLV RAYSMASANH
     EEALEFFSIK VPDGPLTSRL QKIKEGDTIL VGQKPTGTLI TGNLIPGKRL LLLSTGTGLA
     PFASLIKDPE VYENFETIIL AHGCRQTSEL AYGETLVASL LEDELFGPMV KDKLIYYPTV
     TREPFRNRGR ITDLIASAQL FDDVGLPPLN IETDRIMLCG SPGMLEELHD MFEERGFIEG
     SHSEPGHFVI EKAFVER
//