ID   LUXB2_PHOLE             Reviewed;         326 AA.
AC   P29239;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Alkanal monooxygenase beta chain;
DE            EC=1.14.14.3 {ECO:0000269|PubMed:1915359};
DE   AltName: Full=Bacterial luciferase beta chain;
GN   Name=luxB;
OS   Photobacterium leiognathi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=553611;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 25521 / DSM 21260 / CIP 66.5 / NCIMB 2193 / L1;
RX   PubMed=1915359; DOI=10.1111/j.1432-1033.1991.tb16269.x;
RA   Lee C.Y., Szittner R.B., Meighen E.A.;
RT   "The lux genes of the luminous bacterial symbiont, Photobacterium
RT   leiognathi, of the ponyfish. Nucleotide sequence, difference in gene
RT   organization, and high expression in mutant Escherichia coli.";
RL   Eur. J. Biochem. 201:161-167(1991).
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:1915359}.
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:1915359};
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; M63594; AAA25619.1; -; Genomic_DNA.
DR   PIR; S17954; S17954.
DR   RefSeq; WP_023934906.1; NZ_PYOJ01000031.1.
DR   AlphaFoldDB; P29239; -.
DR   SMR; P29239; -.
DR   OrthoDB; 1434838at2; -.
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..326
FT                   /note="Alkanal monooxygenase beta chain"
FT                   /id="PRO_0000220175"
SQ   SEQUENCE   326 AA;  37701 MW;  E7E5C05069B64688 CRC64;
     MNFGLFFLNF QPEGMTSEMV LDNMVDTVAL VDKDDYHFKR VLVSEHHFSK NGIIGEPLTA
     ISFLLGLTKR IEIGSLNQVI TTHHPVRIGE QTGLLDQMSY GRFVLGLSDC VNDFEMDFFK
     RKRSSQQQQF EACYEILNEA LTTNYCQADD DFFNFPRISV NPHCISEVKQ YILASSMGVV
     EWAARKGLPL TYRWSDSLAE KEKYYQRYLA VAKENNIDVS NIDHQFPLLV NINENRRIAR
     DEVREYIQSY VSEAYPTDPN IELRVEELIE QHAVGKVDEY YDSTMHAVKV TGSKNLLLSF
     ESMKNKDDVT KLINMFNQKI KDNLIK