ID   LUXF_PHOPO              Reviewed;         231 AA.
AC   P12745;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Non-fluorescent flavoprotein;
DE            Short=NFP;
DE   AltName: Full=FP390;
GN   Name=luxF;
OS   Photobacterium phosphoreum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3415691; DOI=10.1016/s0006-291x(88)81092-1;
RA   Soly R.R., Mancini J.A., Ferri S.R., Boylan M., Meighen E.A.;
RT   "A new lux gene in bioluminescent bacteria codes for a protein homologous
RT   to the bacterial luciferase subunits.";
RL   Biochem. Biophys. Res. Commun. 155:351-358(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX   PubMed=2018544; DOI=10.1016/0006-291x(91)90959-b;
RA   Ferri S.R., Soly R.R., Szittner R.B., Meighen E.A.;
RT   "Structure and properties of luciferase from Photobacterium phosphoreum.";
RL   Biochem. Biophys. Res. Commun. 176:541-548(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 218-231.
RX   PubMed=2023262; DOI=10.1016/0022-2836(91)90858-4;
RA   Soly R.R., Meighen E.A.;
RT   "Identification of the acyl transfer site of fatty acyl-protein synthetase
RT   from bioluminescent bacteria.";
RL   J. Mol. Biol. 219:69-77(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   PubMed=15299728; DOI=10.1107/s0907444995009796;
RA   Kita A., Kasai S., Miyata M., Miki K.;
RT   "Structure of flavoprotein FP390 from a luminescent bacterium
RT   Photobacterium phosphoreum refined at 2.7-A resolution.";
RL   Acta Crystallogr. D 52:77-86(1996).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M22128; AAA25623.1; -; Genomic_DNA.
DR   EMBL; M65067; AAA70299.1; -; Genomic_DNA.
DR   PIR; A31572; A31572.
DR   PDB; 1FVP; X-ray; 2.70 A; A/B=1-231.
DR   PDBsum; 1FVP; -.
DR   AlphaFoldDB; P12745; -.
DR   SMR; P12745; -.
DR   EvolutionaryTrace; P12745; -.
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; IPR036661; Luciferase-like_sf.
DR   InterPro; IPR002103; Luciferase_bac/NFP.
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..231
FT                   /note="Non-fluorescent flavoprotein"
FT                   /id="PRO_0000220183"
FT   STRAND          6..11
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   HELIX           23..38
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   STRAND          40..48
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   STRAND          65..68
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   STRAND          71..75
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   HELIX           80..87
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   STRAND          96..98
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   HELIX           100..116
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   STRAND          126..130
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   HELIX           138..155
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   HELIX           166..171
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   HELIX           178..190
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   TURN            191..193
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   STRAND          195..199
FT                   /evidence="ECO:0007829|PDB:1FVP"
FT   HELIX           207..227
FT                   /evidence="ECO:0007829|PDB:1FVP"
SQ   SEQUENCE   231 AA;  26606 MW;  87EB6482C2870661 CRC64;
     MNKWNYGVFF VNFYNKGQQE PSKTMNNALE TLRIIDEDTS IYDVINIDDH YLVKKDSEDK
     KLASFITLGE KLYVLATSEN TVDIAAKYAL PLVFKWDDIN EERLKLLSFY NASASKYNKN
     IDLVRHQLML HVNVNEAETV AKEELKLYIE NYVACTQPSN FNGSIDSIIQ SNVTGSYKDC
     LSYVANLAGK FDNTVDFLLC FESMQDQNKK KSVMIDLNNQ VIKFRQDNNL I