LUZ_NEONM
ID LUZ_NEONM Reviewed; 267 AA.
AC A0A3G9JYH7;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Luciferase {ECO:0000303|PubMed:30478037};
DE EC=1.-.-.- {ECO:0000269|PubMed:28508049, ECO:0000269|PubMed:30478037};
DE AltName: Full=Fungal bioluminescence cycle protein luz {ECO:0000303|PubMed:30478037};
GN Name=luz {ECO:0000303|PubMed:30478037};
OS Neonothopanus nambi (Agaricus nambi).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Omphalotaceae; Neonothopanus.
OX NCBI_TaxID=71958;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, PATHWAY, AND
RP 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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28508049; DOI=10.1126/sciadv.1602847;
RA Kaskova Z.M., Doerr F.A., Petushkov V.N., Purtov K.V., Tsarkova A.S.,
RA Rodionova N.S., Mineev K.S., Guglya E.B., Kotlobay A., Baleeva N.S.,
RA Baranov M.S., Arseniev A.S., Gitelson J.I., Lukyanov S., Suzuki Y.,
RA Kanie S., Pinto E., Di Mascio P., Waldenmaier H.E., Pereira T.A.,
RA Carvalho R.P., Oliveira A.G., Oba Y., Bastos E.L., Stevani C.V.,
RA Yampolsky I.V.;
RT "Mechanism and color modulation of fungal bioluminescence.";
RL Sci. Adv. 3:e1602847-e1602847(2017).
CC -!- FUNCTION: Luciferase; part of the gene cluster that mediates the fungal
CC bioluminescence cycle (PubMed:30478037, PubMed:28508049). Uses the
CC fungal luciferin 3-hydroxyhispidin as a substrate to produce an
CC endoperoxide as a high-energy intermediate with decomposition that
CC yields oxyluciferin (also known as caffeoylpyruvate) and light emission
CC (PubMed:30478037, PubMed:28508049). The fungal bioluminescence cycle
CC begins with the hispidin synthetase that catalyzes the formation of
CC hispidin which is further hydroxylated by the hispidin-3-hydroxylase,
CC yielding the fungal luciferin 3-hydroxyhispidin. The luciferase then
CC produces an endoperoxide as a high-energy intermediate with
CC decomposition that yields oxyluciferin and light emission. Oxyluciferin
CC can be recycled to caffeic acid by caffeoylpyruvate hydrolase
CC (PubMed:30478037) (Probable). {ECO:0000269|PubMed:28508049,
CC ECO:0000269|PubMed:30478037, 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:0000269|PubMed:28508049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71144;
CC Evidence={ECO:0000269|PubMed:28508049};
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:0000269|PubMed:28508049};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71148;
CC Evidence={ECO:0000269|PubMed:28508049};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:30478037};
CC Temperature dependence:
CC Optimum temperature is 10 to 18 degrees Celsius.
CC {ECO:0000269|PubMed:30478037};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:30478037}; Single-
CC 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; LC435379; BBH43509.1; -; 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 Glycoprotein; Membrane; Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..267
FT /note="Luciferase"
FT /id="PRO_0000455710"
FT TRANSMEM 17..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 267 AA; 30381 MW; 0E52255B15D23E6D CRC64;
MRINISLSSL FERLSKLSSR SIAITCGVVL ASAIAFPIIR RDYQTFLEVG PSYAPQNFRG
YIIVCVLSLF RQEQKGLAIY DRLPEKRRWL ADLPFREGTR PSITSHIIQR QRTQLVDQEF
ATRELIDKVI PRVQARHTDK TFLSTSKFEF HAKAIFLLPS IPINDPLNIP SHDTVRRTKR
EIAHMHDYHD CTLHLALAAQ DGKEVLKKGW GQRHPLAGPG VPGPPTEWTF LYAPRNEEEA
RVVEMIVEAS IGYMTNDPAG KIVENAK
