H3H_NEONM
ID H3H_NEONM Reviewed; 422 AA.
AC A0A3G9K5C8;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=Hispidin-3-hydroxylase {ECO:0000303|PubMed:30478037};
DE Short=H3H {ECO:0000303|PubMed:30478037};
DE EC=1.-.-.- {ECO:0000269|PubMed:26094784};
DE AltName: Full=FAD-dependent monooxygenase h3h {ECO:0000303|PubMed:30478037};
DE AltName: Full=Fungal bioluminescence cycle protein h3h {ECO:0000303|PubMed:30478037};
GN Name=h3h {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=26094784; DOI=10.1002/anie.201501779;
RA Purtov K.V., Petushkov V.N., Baranov M.S., Mineev K.S., Rodionova N.S.,
RA Kaskova Z.M., Tsarkova A.S., Petunin A.I., Bondar V.S., Rodicheva E.K.,
RA Medvedeva S.E., Oba Y., Oba Y., Arseniev A.S., Lukyanov S., Gitelson J.I.,
RA Yampolsky I.V.;
RT "The chemical basis of fungal bioluminescence.";
RL Angew. Chem. Int. Ed. 54:8124-8128(2015).
CC -!- FUNCTION: Hispidin-3-hydroxylase; part of the gene cluster that
CC mediates the fungal bioluminescence cycle (PubMed:30478037,
CC PubMed:26094784). Hydroxylates hispidin in order to produce the fungal
CC luciferin 3-hydroxyhispidin (PubMed:30478037, PubMed:26094784). 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 (also known as caffeoylpyruvate) and light emission. Oxyluciferin can
CC be recycled to caffeic acid by caffeoylpyruvate hydrolase
CC (PubMed:30478037) (Probable). {ECO:0000269|PubMed:26094784,
CC ECO:0000269|PubMed:30478037, ECO:0000305|PubMed:30478037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hispidin + NADH + O2 = 3-hydroxyhispidin + H2O +
CC NAD(+); Xref=Rhea:RHEA:71115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:190288, ChEBI:CHEBI:190289;
CC Evidence={ECO:0000250|UniProtKB:A0A146I0C4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71116;
CC Evidence={ECO:0000250|UniProtKB:A0A146I0C4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hispidin + NADPH + O2 = 3-hydroxyhispidin + H2O +
CC NADP(+); Xref=Rhea:RHEA:71119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:190288, ChEBI:CHEBI:190289;
CC Evidence={ECO:0000269|PubMed:26094784};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71120;
CC Evidence={ECO:0000269|PubMed:26094784};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:A6T923};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:30478037}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A0A146I0C4}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC 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 paxM FAD-dependent monooxygenase family.
CC {ECO:0000269|PubMed:30478037, ECO:0000305}.
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DR EMBL; LC435367; BBH43497.1; -; mRNA.
DR SMR; A0A3G9K5C8; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Membrane; Monooxygenase; Oxidoreductase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..422
FT /note="Hispidin-3-hydroxylase"
FT /id="PRO_0000455706"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 18
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 37..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 247..249
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 318
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
FT BINDING 328..332
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:A6T923"
SQ SEQUENCE 422 AA; 46449 MW; 3CE9DAD13C0E4A57 CRC64;
MASFENSLSV LIVGAGLGGL AAAIALRRQG HVVKIYDSSS FKAELGAGLA VPPNTLRSLQ
QLGCNTENLN GVDNLCFTAM GYDGSVGMMN NMTDYREAYG TSWIMVHRVD LHNELMRVAL
DPGGLGPPAT LHLNHRVTFC DVDACTVTFT NGTTQSADLI VGADGIRSTI RRFVLEEDVT
VPASGIVGFR WLVQADALDP YPELDWIVKK PPLGARLIST PQNPQSGVGL ADRRTIIIYA
CRGGTMVNVL AVHDDERDQN TADWSVPASK DDLFRVFHDY HPRFRRLLEL AQDINLWQMR
VVPVLKKWVN KRVCLLGDAA HASLPTLGQG FGMGLEDAVA LGTLLPKGTT ASQIETRLAV
YEQLRKDRAE FVAAESYEEQ YVPEMRGLYL RSKELRDRVM GYDIKVESEK VLETLLRSSN
SA
