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LUXA2_PHOLU
ID   LUXA2_PHOLU             Reviewed;         362 AA.
AC   P23146;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Alkanal monooxygenase alpha chain;
DE            EC=1.14.14.3 {ECO:0000269|PubMed:1995589};
DE   AltName: Full=Bacterial luciferase alpha chain;
GN   Name=luxA;
OS   Photorhabdus luminescens (Xenorhabdus luminescens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=29488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Hw;
RX   PubMed=1995589; DOI=10.1128/jb.173.4.1399-1405.1991;
RA   Xi L., Cho K.W., Tu S.C.;
RT   "Cloning and nucleotide sequences of lux genes and characterization of
RT   luciferase of Xenorhabdus luminescens from a human wound.";
RL   J. Bacteriol. 173:1399-1405(1991).
CC   -!- FUNCTION: Light-emitting reaction in luminous bacteria.
CC       {ECO:0000269|PubMed:1995589}.
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:1995589};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- MISCELLANEOUS: The synthesis of this protein is regulated by a complex
CC       control mechanism that has been termed autoinduction.
CC   -!- SIMILARITY: Belongs to the bacterial luciferase oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; M62917; AAA63565.1; -; Genomic_DNA.
DR   PIR; C38448; C38448.
DR   AlphaFoldDB; P23146; -.
DR   SMR; P23146; -.
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; -; 1.
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..362
FT                   /note="Alkanal monooxygenase alpha chain"
FT                   /id="PRO_0000220168"
SQ   SEQUENCE   362 AA;  41401 MW;  6F9033401D296416 CRC64;
     MKFGNFLLTY QPPQFSQTEV MKWLVKLGRI SEECGFDTVW LLEHHFTEFG LLGNPYVAAA
     YLLGATKKLN VGTAAIVLPT AHPVRQLEEV NLLDQMSKGR FRFGICRGLY NKDFRVFGTD
     MNNSRALMEC WYKLIRNGMT EGYMEADNEH IKFHKVKVLP TAYSQGGAPI YVVAESASTT
     EWAAQHGLPM ILSWIINTND KKAQIELYNE VAQEYGHDIH NIDHCLSYIT SVDHDSMKAK
     EICRNFLGHW YDSYVNATTI FDDSDKTKGY DFNKGQWRDF VLKGHKNTNR RVDYSYEINP
     VGTPQECIDI IQTDIDATGI SNICCGFEAN GTVDEIISSM KLFQSDVMPF LKEKQQFSYY
     IS
 
 
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