ID   LUXA2_PHOLE             Reviewed;         354 AA.
AC   P29238;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Alkanal monooxygenase alpha chain;
DE            EC=1.14.14.3 {ECO:0000269|PubMed:1915359};
DE   AltName: Full=Bacterial luciferase alpha chain;
GN   Name=luxA;
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.
CC       {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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M63594; AAA25618.1; -; Genomic_DNA.
DR   PIR; S17953; S17953.
DR   RefSeq; WP_023934905.1; NZ_PYOJ01000031.1.
DR   AlphaFoldDB; P29238; -.
DR   SMR; P29238; -.
DR   PRIDE; P29238; -.
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; -; 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..354
FT                   /note="Alkanal monooxygenase alpha chain"
FT                   /id="PRO_0000220165"
SQ   SEQUENCE   354 AA;  40402 MW;  07001C2064F4645B CRC64;
     MKISNICFSY QPPGESHQEV MERFIRLGVA SEELNFDGFY TLEHHFTEFG ITGNLYIACA
     NILGRTKRIQ VGTMGIVLPT EHPARHVESL LVLDQLSKGR FNYGTVRGLY HKDFRVFGTS
     QEDSRKTAEN FYSMILDASK TGVLHTDGEV VEFPDVNVYP EAYSKKQPTC MTAESSETIT
     YLAERGLPMV LSWIIPVSEK VSQMELYNEV AAEHGHDINN IEHILTFICS VNEDGEKADS
     VCRNFLENWY DSYKNATNIF NDSNQTRGYD YLKAQWREWV MKGLADPRRR LDYSNELNPV
     GTPERCIEII QSNIDATGIK HITVGFEANG SEQEIRESME LFMEKVAPHL KDPQ