ID   LUXB_ALIFS              Reviewed;         326 AA.
AC   P19908;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Alkanal monooxygenase beta chain;
DE            EC=1.14.14.3 {ECO:0000250|UniProtKB:P12744};
DE   AltName: Full=Bacterial luciferase beta chain;
GN   Name=luxB;
OS   Aliivibrio fischeri (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MJ-1;
RX   PubMed=3340562; DOI=10.1093/nar/16.2.777;
RA   Foran D.R., Brown W.M.;
RT   "Nucleotide sequence of the LuxA and LuxB genes of the bioluminescent
RT   marine bacterium Vibrio fischeri.";
RL   Nucleic Acids Res. 16:777-777(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MJ-1;
RA   Knight T., Papadakis N.;
RT   "Vibrio fischeri Lux operon SalI digest.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P12744}.
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:0000250|UniProtKB:P12744};
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; X06758; CAA29932.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U55385; AAB00443.1; -; Genomic_DNA.
DR   EMBL; U55819; AAB00450.1; -; Genomic_DNA.
DR   EMBL; AF170104; AAD48478.1; -; Genomic_DNA.
DR   PIR; S00575; S00575.
DR   RefSeq; WP_005423450.1; NZ_WOBZ01000007.1.
DR   AlphaFoldDB; P19908; -.
DR   SMR; P19908; -.
DR   BioCyc; MetaCyc:LUXBVIBFI-MON; -.
DR   BRENDA; 1.14.14.3; 71.
DR   GO; GO:0047646; F:alkanal monooxygenase (FMN-linked) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IMP:CACAO.
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   3: Inferred from homology;
KW   Flavoprotein; FMN; Luminescence; Monooxygenase; Oxidoreductase;
KW   Photoprotein.
FT   CHAIN           1..326
FT                   /note="Alkanal monooxygenase beta chain"
FT                   /id="PRO_0000220180"
SQ   SEQUENCE   326 AA;  37357 MW;  228C0FB433F79F75 CRC64;
     MKFGLFFLNF QKDGITSEET LDNMVKTVTL IDSTKYHFNT AFVNEHHFSK NGIVGAPITA
     AGFLLGLTNK LHIGSLNQVI TTHHPVRVAE EASLLDQMSE GRFILGFSDC ESDFEMEFFR
     RHISSRQQQF EACYEIINDA LTTGYCHPQN DFYDFPKVSI NPHCYSENGP KQYVSATSKE
     VVMWAAKKAL PLTFKWEDNL ETKERYAILY NKTAQQYGID ISDVDHQLTV IANLNADRST
     AQEEVREYLK DYITETYPQM DRDEKINCII EENAVGSHDD YYESTKLAVE KTGSKNILLS
     FESMSDIKDV KDIIDMLNQK IEMNLP