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Database: UniProt
Entry: E4ZD64_NEIL0
LinkDB: E4ZD64_NEIL0
Original site: E4ZD64_NEIL0 
ID   E4ZD64_NEIL0            Unreviewed;       258 AA.
AC   E4ZD64;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   Name=fpr {ECO:0000313|EMBL:CBN87297.1};
GN   OrderedLocusNames=NLA_10740 {ECO:0000313|EMBL:CBN87297.1};
OS   Neisseria lactamica (strain 020-06).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=489653 {ECO:0000313|EMBL:CBN87297.1, ECO:0000313|Proteomes:UP000008723};
RN   [1] {ECO:0000313|EMBL:CBN87297.1, ECO:0000313|Proteomes:UP000008723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=020-06 {ECO:0000313|EMBL:CBN87297.1,
RC   ECO:0000313|Proteomes:UP000008723};
RX   PubMed=21092259; DOI=10.1186/1471-2164-11-652;
RA   Bennett J.S., Bentley S.D., Vernikos G.S., Quail M.A., Cherevach I.,
RA   White B., Parkhill J., Maiden M.C.;
RT   "Independent evolution of the core and accessory gene sets in the genus
RT   Neisseria: insights gained from the genome of Neisseria lactamica isolate
RT   020-06.";
RL   BMC Genomics 11:652-652(2010).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR   EMBL; FN995097; CBN87297.1; -; Genomic_DNA.
DR   RefSeq; WP_003714053.1; NC_014752.1.
DR   AlphaFoldDB; E4ZD64; -.
DR   KEGG; nla:NLA_10740; -.
DR   eggNOG; COG0543; Bacteria.
DR   HOGENOM; CLU_003827_3_0_4; -.
DR   Proteomes; UP000008723; 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   Oxidoreductase {ECO:0000313|EMBL:CBN87297.1}.
FT   DOMAIN          2..102
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   258 AA;  29319 MW;  ADAD6B8A80AC3C52 CRC64;
     MAAFNTQKVL SVHHWTDAYF TFTCTRDESL RFENGQFVMV GLMVDGKPLM RAYSVASANW
     EEHLEFFSIK VQDGPLTSRL QHLKVGDDVL ISKKPTGTLV AGDLNPGKHL YLLSTGTGIA
     PFLSITKDPE IYEQFEKIIL VHGVRYKKDL AYYDRFTKEL PEHEYLGDLV KEKLIYYPIV
     SREDFEHRGR LTDLMVSGKL FEDIGLPKIN PQDDRAMLCG SPAMLKDTCK VLDDFGLTVS
     PKTGVRGDYL IERAFVDQ
//
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