ID   LUXB_PHOPO              Reviewed;         318 AA.
AC   P12744;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Alkanal monooxygenase beta chain;
DE            EC=1.14.14.3 {ECO:0000269|PubMed:2018544};
DE   AltName: Full=Bacterial luciferase beta chain;
GN   Name=luxB;
OS   Photobacterium phosphoreum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
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   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-318.
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).
CC   -!- FUNCTION: Light-emitting reaction in luminous bacteria. The specific
CC       role of the beta subunit is unknown, but it is absolutely required for
CC       bioluminescence activity. {ECO:0000269|PubMed:2018544}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty aldehyde + FMNH2 + O2 = a long-chain fatty
CC         acid + FMN + 2 H(+) + H2O + hnu; Xref=Rhea:RHEA:17181,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17176, ChEBI:CHEBI:30212, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.3;
CC         Evidence={ECO:0000269|PubMed:2018544};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000250|UniProtKB:P07740}.
CC   -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; M65067; AAA70298.1; -; Genomic_DNA.
DR   EMBL; M22128; AAA25622.1; -; Genomic_DNA.
DR   PIR; JH0388; JH0388.
DR   AlphaFoldDB; P12744; -.
DR   SMR; P12744; -.
DR   STRING; 659.AYY26_10980; -.
DR   PRIDE; P12744; -.
DR   GO; GO:0047646; F:alkanal monooxygenase (FMN-linked) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR   CDD; cd01096; Alkanal_monooxygenase; 1.
DR   Gene3D; 3.20.20.30; -; 2.
DR   InterPro; IPR033924; Alkanal_monooxygenase.
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   Flavoprotein; FMN; Luminescence; Monooxygenase; Oxidoreductase;
KW   Photoprotein.
FT   CHAIN           1..318
FT                   /note="Alkanal monooxygenase beta chain"
FT                   /id="PRO_0000220179"
FT   CONFLICT        307
FT                   /note="M -> MV (in Ref. 2; AAA25622)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   318 AA;  36397 MW;  9ECAE7C176A72C04 CRC64;
     MNFGLFFLNF PENTSSETVL DNMINTVSLV DKDYKNFTTA LVNHHFSKNG IVGAPMTAAS
     FLLGLTERLH IGSLNQITTH HPVRIAEEAS LLDQMSDSRF ILGLSDCVNF EMDFFKRQRD
     SQQLQFEACY DIINEAITTN YCANNDFYNF PRISINPHCL SKENMKQYIL ASSVSVEWAA
     KKALPLTYRW SDTLEDKEIL YKRYLEVAKH NIDVSNVEHQ FPLLVNLNHD RDVAHQEATA
     YVSYIAEVYP HLNQQQKIAE LISQHAIGTD NDYYSTLNAL ERTGSKNVLL SFESMKNHDD
     VVKVINMNEK IQKNLPSS