ID   LUZ_ARMOS               Reviewed;         266 AA.
AC   A0A3G9K3N1;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 5.
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 ostoyae (Armillaria root rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Physalacriaceae; Armillaria.
OX   NCBI_TaxID=47428;
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; LC435375; BBH43505.1; -; mRNA.
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_0000455709"
FT   TRANSMEM        22..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   266 AA;  29794 MW;  EC896C5B594D3F34 CRC64;
     MSFIDSMKLD FVGHLFGIRN RGLATACCAV AVASAIAFPY IRRDYQTFLS GGPSYAPQNI
     KGYLIVCVLA LFRQEQKGLA IYDRLPEKRR WLPDLPPRNG PRPITTSHII QRQRNQAPDS
     KFALEELKAT VIPRVQARHT DLTHLSLSKF EFHAEAIFLL PSVPIDDPKN VPSHDTVRRT
     KREIAHMHDY HDFTLHLALA AQDGKEVVAK GWGQRHPLAG PGVPGPPTEW TFIYAPRNEE
     ELAVVEMIIE ASIGYMTNDP AGTVIV