ID   LUXA_PHOPO              Reviewed;         346 AA.
AC   P24113;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Alkanal monooxygenase alpha chain;
DE            EC=1.14.14.3 {ECO:0000269|PubMed:2018544};
DE   AltName: Full=Bacterial luciferase alpha chain;
GN   Name=luxA;
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 1-41.
RX   PubMed=2071574; DOI=10.1016/s0021-9258(18)98772-7;
RA   Ferri S.R., Meighen E.A.;
RT   "A lux-specific myristoyl transferase in luminescent bacteria related to
RT   eukaryotic serine esterases.";
RL   J. Biol. Chem. 266:12852-12857(1991).
CC   -!- FUNCTION: Light-emitting reaction in luminous bacteria.
CC       {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}.
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DR   EMBL; M65067; AAA70297.1; -; Genomic_DNA.
DR   EMBL; M64224; AAA25627.1; -; Genomic_DNA.
DR   PIR; JH0387; JH0387.
DR   AlphaFoldDB; P24113; -.
DR   SMR; P24113; -.
DR   STRING; 659.AYY26_10985; -.
DR   GO; GO:0047646; F:alkanal monooxygenase (FMN-linked) activity; IEA:UniProtKB-EC.
DR   GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
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   Flavoprotein; FMN; Luminescence; Monooxygenase; Oxidoreductase;
KW   Photoprotein.
FT   CHAIN           1..346
FT                   /note="Alkanal monooxygenase alpha chain"
FT                   /id="PRO_0000220169"
FT   CONFLICT        6
FT                   /note="I -> IC (in Ref. 2; AAA25627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40..41
FT                   /note="LE -> TL (in Ref. 2; AAA25627)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   346 AA;  39364 MW;  360EC324E0A438A0 CRC64;
     MKFGNIFSYQ PPGESHKEVM DRFVRLGVAS EELNFDTYWL EHHFTEFGLT GNLFVACANL
     LGRTTKLNVG TMIVLPTAHP ARQMEDLLLL DQMSKGRFNF GVVRGYHKDF RVFGVTMEDS
     RAITEDFHTM IMDGTKTGLH TDGKNIEFPD VNVYPEAYLE KIPTCMTAES ATTTWLAERG
     LPMVLSWIIT TSEKKAQMEL YNAVRDSGYS EEYIKNVDHS MTLICSVDED GKKAEDVREF
     LGNWYDSYVN ATNIFSESNQ TRGYDYHKGQ KDFVLQGHTN TKRRVDYSND LNPVGTPEKC
     IEIQRDIDAT GITNITLGFE ANGSEEEIIA SMKRFMQVAP FLKDPK