ID   LUZ_ARMME               Reviewed;         266 AA.
AC   A0A3G9JTR4;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 6.
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};
OS   Armillaria mellea (Shoestring root rot fungus) (Honey mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47429;
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).
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; LC435374; BBH43504.1; -; mRNA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR040841; DUF5519.
DR   Pfam; PF17648; DUF5519; 1.
PE   1: Evidence at protein level;
KW   Membrane; Oxidoreductase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..266
FT                   /note="Luciferase"
FT                   /id="PRO_0000455707"
FT   TRANSMEM        22..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   266 AA;  29939 MW;  CD811F4BAFCDDC6E CRC64;
     MSFFDSVKLD LVGRLFGIRN RGLAVTCCAV AVASIIAFPY IRRDYQTFLS GGPSYAPQNI
     RGYLIVCVLA LFRQEQKGLA IYDRLPEKRR WLPDLPPRDG PRPITTSHII QRQRNQAPDL
     KFALEELKAT VIPRVQARHT DLTHLSLSKF EFHAEAIFLL PSVPIDDPKN VPSHDTVRRT
     KREIAHMHDY HDYTLHLALA AQDGKEVVSK GWGQRHPLAG PGVPGPPTEW TFIYAPRNEE
     ELAVVEMIIE ASIGYMTNDP AGKTIA