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Database: UniProt
Entry: I8HXY3_9GAMM
LinkDB: I8HXY3_9GAMM
Original site: I8HXY3_9GAMM 
ID   I8HXY3_9GAMM            Unreviewed;       258 AA.
AC   I8HXY3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=ferredoxin--NADP(+) reductase {ECO:0000256|ARBA:ARBA00013223};
DE            EC=1.18.1.2 {ECO:0000256|ARBA:ARBA00013223};
GN   ORFNames=WQQ_35060 {ECO:0000313|EMBL:EIT68311.1};
OS   Hydrocarboniphaga effusa AP103.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC   Hydrocarboniphaga.
OX   NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT68311.1, ECO:0000313|Proteomes:UP000003704};
RN   [1] {ECO:0000313|EMBL:EIT68311.1, ECO:0000313|Proteomes:UP000003704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP103 {ECO:0000313|EMBL:EIT68311.1,
RC   ECO:0000313|Proteomes:UP000003704};
RX   PubMed=22933753; DOI=10.1128/JB.01017-12;
RA   Chang H.K., Zylstra G.J., Chae J.C.;
RT   "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT   AP103T (ATCC BAA-332T).";
RL   J. Bacteriol. 194:5120-5120(2012).
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:EIT68311.1}.
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DR   EMBL; AKGD01000003; EIT68311.1; -; Genomic_DNA.
DR   RefSeq; WP_007186445.1; NZ_AKGD01000003.1.
DR   AlphaFoldDB; I8HXY3; -.
DR   STRING; 1172194.WQQ_35060; -.
DR   PATRIC; fig|1172194.4.peg.3403; -.
DR   OrthoDB; 9784483at2; -.
DR   Proteomes; UP000003704; 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   PRINTS; PR00410; PHEHYDRXLASE.
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:UP000003704}.
FT   DOMAIN          2..102
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   258 AA;  29324 MW;  DA27441EDA4B0040 CRC64;
     MAAIGKEKIL SVRHWNDTLF SFTATRDPAL RFENGHFVMI GLEVNGKPLM RAYSIASANY
     EEHLEFFSIK VQDGPLTSRL QHLKVGDELL VSRKPTGTLV LHDLKPGKHL YMLSTGTGLA
     PFLSLVKDPE TYERFEKIVL IHGVRYVNEL AYQQFFRQEL REHEFLGEQV KEKLIYYPTV
     TREDYQNTGR LTDLIESGKL FSDIGLPRFD PAVDRAMICG SPSMLKDSSA LLDAHGLRIS
     PHIGQPGDYV IERAFVEK
//
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