ID   LUZ_ARMGA               Reviewed;         266 AA.
AC   A0A2H3E985;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2018, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Luciferase {ECO:0000303|PubMed:30478037};
DE            EC=1.-.-.- {ECO:0000269|PubMed:30478037};
DE   AltName: Full=Fungal bioluminescence cycle protein luz {ECO:0000303|PubMed:30478037};
GN   Name=luz {ECO:0000303|PubMed:30478037}; ORFNames=ARMGADRAFT_268845;
OS   Armillaria gallica (Bulbous honey fungus) (Armillaria bulbosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47427;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, FUNCTION, AND BIOTECHNOLOGY.
RX   PubMed=30478037; DOI=10.1073/pnas.1803615115;
RA   Kotlobay A.A., Sarkisyan K.S., Mokrushina Y.A., Marcet-Houben M.,
RA   Serebrovskaya E.O., Markina N.M., Gonzalez Somermeyer L.,
RA   Gorokhovatsky A.Y., Vvedensky A., Purtov K.V., Petushkov V.N.,
RA   Rodionova N.S., Chepurnyh T.V., Fakhranurova L.I., Guglya E.B.,
RA   Ziganshin R., Tsarkova A.S., Kaskova Z.M., Shender V., Abakumov M.,
RA   Abakumova T.O., Povolotskaya I.S., Eroshkin F.M., Zaraisky A.G.,
RA   Mishin A.S., Dolgov S.V., Mitiouchkina T.Y., Kopantzev E.P.,
RA   Waldenmaier H.E., Oliveira A.G., Oba Y., Barsova E., Bogdanova E.A.,
RA   Gabaldon T., Stevani C.V., Lukyanov S., Smirnov I.V., Gitelson J.I.,
RA   Kondrashov F.A., Yampolsky I.V.;
RT   "Genetically encodable bioluminescent system from fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:12728-12732(2018).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ar21-2;
RX   PubMed=29085064; DOI=10.1038/s41559-017-0347-8;
RA   Sipos G., Prasanna A.N., Walter M.C., O'Connor E., Balint B., Krizsan K.,
RA   Kiss B., Hess J., Varga T., Slot J., Riley R., Boka B., Rigling D.,
RA   Barry K., Lee J., Mihaltcheva S., LaButti K., Lipzen A., Waldron R.,
RA   Moloney N.M., Sperisen C., Kredics L., Vagvoelgyi C., Patrignani A.,
RA   Fitzpatrick D., Nagy I., Doyle S., Anderson J.B., Grigoriev I.V.,
RA   Gueldener U., Muensterkoetter M., Nagy L.G.;
RT   "Genome expansion and lineage-specific genetic innovations in the forest
RT   pathogenic fungi Armillaria.";
RL   Nat. Ecol. Evol. 1:1931-1941(2017).
CC   -!- FUNCTION: Luciferase; part of the gene cluster that mediates the fungal
CC       bioluminescence cycle (PubMed:30478037). Uses the fungal luciferin 3-
CC       hydroxyhispidin as a substrate to produce an endoperoxide as a high-
CC       energy intermediate with decomposition that yields oxyluciferin (also
CC       known as caffeoylpyruvate) and light emission (By similarity). The
CC       fungal bioluminescence cycle begins with the hispidin synthetase that
CC       catalyzes the formation of hispidin which is further hydroxylated by
CC       the hispidin-3-hydroxylase, yielding the fungal luciferin 3-
CC       hydroxyhispidin. The luciferase then produces an endoperoxide as a
CC       high-energy intermediate with decomposition that yields oxyluciferin
CC       and light emission. Oxyluciferin can be recycled to caffeic acid by
CC       caffeoylpyruvate hydrolase (PubMed:30478037) (Probable).
CC       {ECO:0000250|UniProtKB:A0A3G9JYH7, ECO:0000269|PubMed:30478037,
CC       ECO:0000305|PubMed:30478037}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxyhispidin + O2 = (E)-caffeoylpyruvate + CO2 + hnu;
CC         Xref=Rhea:RHEA:71143, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:30212, ChEBI:CHEBI:190289, ChEBI:CHEBI:190290;
CC         Evidence={ECO:0000250|UniProtKB:A0A3G9JYH7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71144;
CC         Evidence={ECO:0000250|UniProtKB:A0A3G9JYH7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-hydroxyhispidin + O2 = 4-[(E)-2-(3,4-
CC         dihydroxyphenyl)ethenyl]-1,7-dihydroxy-2,3,5-trioxabicyclo[2.2.2]oct-
CC         7-en-6-one; Xref=Rhea:RHEA:71147, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:190289, ChEBI:CHEBI:190291;
CC         Evidence={ECO:0000250|UniProtKB:A0A3G9JYH7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71148;
CC         Evidence={ECO:0000250|UniProtKB:A0A3G9JYH7};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:A0A3G9JYH7};
CC       Single-pass membrane protein {ECO:0000255}.
CC   -!- BIOTECHNOLOGY: The availability of a complete eukaryotic luciferin
CC       biosynthesis pathway provides several applications in biomedicine and
CC       bioengineering. {ECO:0000269|PubMed:30478037}.
CC   -!- SIMILARITY: Belongs to the fungal luciferase family. {ECO:0000305}.
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DR   EMBL; LC435373; BBH43503.1; -; mRNA.
DR   EMBL; KZ293645; PBL02715.1; -; Genomic_DNA.
DR   EnsemblFungi; PBL02715; PBL02715; ARMGADRAFT_268845.
DR   OMA; MYREIGH; -.
DR   OrthoDB; 1476777at2759; -.
DR   Proteomes; UP000217790; Unassembled WGS sequence.
DR   InterPro; IPR040841; DUF5519.
DR   Pfam; PF17648; DUF5519; 1.
PE   1: Evidence at protein level;
KW   Membrane; Oxidoreductase; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..266
FT                   /note="Luciferase"
FT                   /id="PRO_0000455708"
FT   TRANSMEM        22..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   266 AA;  29832 MW;  E9983F6C31090C3A CRC64;
     MSFIDSMKLD LVGHLFGIRN RGLAAACCAL AVASTIAFPY IRRDYQTFLS GGPSYAPQNI
     RGYFIVCVLA LFRQEQKGLA IYDRLPEKRR WLPDLPPRNG PRPITTSHII QRQRNQAPDP
     KFALEELKAT VIPRVQARHT DLTHLSLSKF EFHAEAIFLL PSVPIDDPKN VPSHDTVRRT
     KREIAHMHDY HDFTLHLALA AQDGKEVVSK GWGQRHPLAG PGVPGPPTEW TFIYAPRNEE
     ELAVVEMIIE ASIGYMTNDP AGVVIA