ID D3HNE7_LEGLN Unreviewed; 233 AA.
AC D3HNE7;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Putative C-terminal part of NAD(P)H-flavin reductase {ECO:0000313|EMBL:CBJ10410.1};
GN OrderedLocusNames=LLO_0085 {ECO:0000313|EMBL:CBJ10410.1};
OS Legionella longbeachae serogroup 1 (strain NSW150).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=661367 {ECO:0000313|EMBL:CBJ10410.1, ECO:0000313|Proteomes:UP000001060};
RN [1] {ECO:0000313|EMBL:CBJ10410.1, ECO:0000313|Proteomes:UP000001060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NSW150 {ECO:0000313|EMBL:CBJ10410.1,
RC ECO:0000313|Proteomes:UP000001060};
RX PubMed=20174605; DOI=10.1371/journal.pgen.1000851;
RA Cazalet C., Gomez-Valero L., Rusniok C., Lomma M., Dervins-Ravault D.,
RA Newton H., Sansom F., Jarraud S., Zidane N., Ma L., Bouchier C.,
RA Etienne J., Hartland E., Buchrieser C.;
RT "Analysis of the Legionella longbeachae genome and transcriptome uncovers
RT unique strategies to cause Legionnaires' disease.";
RL PLoS Genet. 6:E1000851-E1000851(2010).
CC -!- SIMILARITY: Belongs to the Fre/LuxG FAD/NAD(P) flavoprotein
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00038177}.
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DR EMBL; FN650140; CBJ10410.1; -; Genomic_DNA.
DR RefSeq; WP_003633704.1; NC_013861.1.
DR AlphaFoldDB; D3HNE7; -.
DR STRING; 661367.LLO_0085; -.
DR KEGG; llo:LLO_0085; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_7_4_6; -.
DR OrthoDB; 9806195at2; -.
DR Proteomes; UP000001060; Chromosome.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR CDD; cd06189; flavin_oxioreductase; 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; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR47354:SF7; NAD(P)H-FLAVIN REDUCTASE; 1.
DR PANTHER; PTHR47354; NADH OXIDOREDUCTASE HCR; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
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 3: Inferred from homology;
KW Luminescence {ECO:0000256|ARBA:ARBA00023223};
KW Reference proteome {ECO:0000313|Proteomes:UP000001060}.
FT DOMAIN 3..100
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 233 AA; 26709 MW; 6DF8227012D0DCB2 CRC64;
MKEKIIKAQV EDISPLTDSI MRVVLAPERY LDYQAGQYLQ IVFDQDEFSY SIANAPLGSH
KYELHIRHSL ENPYTQRLFA HIKEHGFVNI RLPFGVCSIE HLDAQRPIIF IAGGTGFAPV
KAMIEQLLAT SDTRPFELFW GARLQSDLYL DEKVNSWNTH VSRFNYFSSV SEDNSKPLAS
LVLDRHPRDL NQWQIVISGP FDMVYSTRDA LVNKGVSPEH LFSDAFSFEI KKT
//
