ID   LUXF_PHOLE              Reviewed;         228 AA.
AC   P09142;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Non-fluorescent flavoprotein;
DE            Short=NFP;
DE   AltName: Full=FP390;
GN   Name=luxF;
OS   Photobacterium leiognathi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=553611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=554;
RX   PubMed=3186447; DOI=10.1093/nar/16.20.9855;
RA   Illiarinov B.A., Protopopova M.V., Karginov V.A., Mertvetsov N.P.,
RA   Gitelson J.I.;
RT   "Nucleotide sequence of part of Photobacterium leiognathi lux region.";
RL   Nucleic Acids Res. 16:9855-9855(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=554;
RX   PubMed=2311938; DOI=10.1016/0378-1119(90)90117-a;
RA   Illarionov B.A., Blinov V.M., Donchenko A.P., Protopopova M.V.,
RA   Karginov V.A., Mertvetsov N.P., Gitelson J.I.;
RT   "Isolation of bioluminescent functions from Photobacterium leiognathi:
RT   analysis of luxA, luxB, luxG and neighboring genes.";
RL   Gene 86:89-94(1990).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=8491169; DOI=10.1002/j.1460-2075.1993.tb05824.x;
RA   Moore S.A., James M.N.G., O'Kane D.J., Lee J.;
RT   "Crystal structure of a flavoprotein related to the subunits of bacterial
RT   luciferase.";
RL   EMBO J. 12:1767-1774(1993).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX   PubMed=7776372; DOI=10.1006/jmbi.1995.0289;
RA   Moore S.A., James M.N.G.;
RT   "Structural refinement of the non-fluorescent flavoprotein from
RT   Photobacterium leiognathi at 1.60-A resolution.";
RL   J. Mol. Biol. 249:195-214(1995).
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 2 FMN per subunit. Each FMN has a myristate attached. This
CC       flavin-fatty acid linkage is probably the result of an enzyme-catalyzed
CC       reaction, most likely the bioluminescence reaction itself.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally termed luxG. {ECO:0000305}.
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DR   EMBL; X08036; CAA30833.1; -; Genomic_DNA.
DR   PIR; JQ0415; JQ0415.
DR   PDB; 1NFP; X-ray; 1.60 A; A=1-228.
DR   PDB; 4J2P; X-ray; 1.85 A; A=1-228.
DR   PDBsum; 1NFP; -.
DR   PDBsum; 4J2P; -.
DR   AlphaFoldDB; P09142; -.
DR   SMR; P09142; -.
DR   STRING; 553611.GCA_001557755_01579; -.
DR   DrugBank; DB08231; Myristic acid.
DR   PRIDE; P09142; -.
DR   BRENDA; 1.14.14.3; 4778.
DR   EvolutionaryTrace; P09142; -.
DR   GO; GO:0047646; F:alkanal monooxygenase (FMN-linked) activity; IEA:InterPro.
DR   Gene3D; 3.20.20.30; -; 1.
DR   InterPro; IPR018235; Bacterial_luciferase_CS.
DR   InterPro; IPR011251; Luciferase-like_dom.
DR   InterPro; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR002103; Luciferase_bac/NFP.
DR   Pfam; PF00296; Bac_luciferase; 1.
DR   PRINTS; PR00089; LUCIFERASE.
DR   SUPFAM; SSF51679; SSF51679; 1.
DR   PROSITE; PS00494; BACTERIAL_LUCIFERASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Flavoprotein.
FT   CHAIN           1..228
FT                   /note="Non-fluorescent flavoprotein"
FT                   /id="PRO_0000220182"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   HELIX           21..37
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   HELIX           51..54
FT                   /evidence="ECO:0007829|PDB:4J2P"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   HELIX           79..87
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   HELIX           100..117
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   STRAND          126..134
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   HELIX           138..156
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   HELIX           159..161
FT                   /evidence="ECO:0007829|PDB:4J2P"
FT   HELIX           162..167
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   STRAND          169..172
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   HELIX           174..187
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   TURN            188..190
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   STRAND          192..197
FT                   /evidence="ECO:0007829|PDB:1NFP"
FT   HELIX           204..224
FT                   /evidence="ECO:0007829|PDB:1NFP"
SQ   SEQUENCE   228 AA;  26239 MW;  A4AFDB334B12B54B CRC64;
     MTKWNYGVFF LNFYHVGQQE PSLTMSNALE TLRIIDEDTS IYDVVAFSEH HIDKSYNDET
     KLAPFVSLGK QIHILATSPE TVVKAAKYGM PLLFKWDDSQ QKRIELLNHY QAAAAKFNVD
     IAGVRHRLML FVNVNDNPTQ AKAELSIYLE DYLSYTQAET SIDEIINSNA AGNFDTCLHH
     VAEMAQGLNN KVDFLFCFES MKDQENKKSL MINFDKRVIN YRKEHNLN