ID   CPH_NEONM               Reviewed;         289 AA.
AC   A0A3G9JYJ6;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   13-FEB-2019, sequence version 1.
DT   03-AUG-2022, entry version 8.
DE   RecName: Full=Caffeoylpyruvate hydrolase {ECO:0000303|PubMed:30478037};
DE            Short=CPH {ECO:0000303|PubMed:30478037};
DE            EC=3.7.-.- {ECO:0000269|PubMed:28508049};
DE   AltName: Full=Fungal bioluminescence cycle protein cph {ECO:0000303|PubMed:30478037};
GN   Name=cph {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, 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: Caffeoylpyruvate hydrolase; part of the gene cluster that
CC       mediates the fungal bioluminescence cycle (PubMed:30478037,
CC       PubMed:28508049). Involved in the recycling of oxyluciferin, a pyruvic
CC       acid adduct of caffeic acid, to caffeic acid (PubMed:30478037,
CC       PubMed:28508049). The fungal bioluminescence cycle begins with the
CC       hispidin synthetase that catalyzes the formation of hispidin which is
CC       further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal
CC       luciferin 3-hydroxyhispidin. The luciferase then produces an
CC       endoperoxide as a high-energy intermediate with decomposition that
CC       yields oxyluciferin (also known as caffeoylpyruvate) and light
CC       emission. Oxyluciferin can be recycled to caffeic acid by
CC       caffeoylpyruvate hydrolase (PubMed:30478037) (Probable).
CC       {ECO:0000269|PubMed:28508049, ECO:0000269|PubMed:30478037,
CC       ECO:0000305|PubMed:30478037}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-caffeoylpyruvate + H2O = (E)-caffeate + H(+) + pyruvate;
CC         Xref=Rhea:RHEA:71155, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57770, ChEBI:CHEBI:190290;
CC         Evidence={ECO:0000269|PubMed:28508049};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71156;
CC         Evidence={ECO:0000269|PubMed:28508049};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q6P587};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:Q6P587};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:30478037}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q6P587}.
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 FAH family. {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; LC435389; BBH43519.1; -; mRNA.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.850.10; -; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Metal-binding.
FT   CHAIN           1..289
FT                   /note="Caffeoylpyruvate hydrolase"
FT                   /id="PRO_0000455705"
FT   BINDING         140
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
FT   BINDING         142
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
FT   BINDING         171
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250|UniProtKB:Q6P587"
SQ   SEQUENCE   289 AA;  31419 MW;  FDF0501E5CC6D535 CRC64;
     MAPISSTWSR LIRFVAIETS LVHIGEPIDA TMDVGLARRE GKTIQAYEII GSGSALDLSA
     QVSKNVLTVR ELLMPLSREE IKTVRCLGLN YPVHATEANV AVPKFPNLFY KPVTSLIGPD
     GLITIPSVVQ PPKEHQSDYE AELVIVIGKA AKNVSEDEAL DYVLGYTAAN DISFRKHQLA
     VSQWSFSKGF GSLLLTIRMA QTHSGNINRF SRDQIFNVKK TISFLSQGTT LEPGSIILTG
     TPDGVGFVRN PPLYLKDGDE VMTWIGSGIG TLANTVQEEK TCFASGGHE