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Gene_locus Report for: renre-luc

Renilla reniformis luciferase , luciferin 2-monooxygenase

Comment
Luciferase from Renilla reniformis (RLuc) catalyzes the degradation of coelenterazine in the presence of molecular oxygen, resulting in the product coelenteramide, carbon dioxide, and the desired photon of light (EC 1.13.12.5). This enzyme belongs to the Haloalkane dehalogenase family II with a different catalytic function (EC 3.8.1.5) Reconstruction of an ancestral enzyme shows it has both hydrolase and monooxygenase activities ( Chaloupkova et al.). This luciferase produces light with a wavelength of 480 nm. In presence of a green fluorescence protein (GFP) it produces a green fluorescence at 509 nm. It is differnt of most other luciferases which are not alpha Beta hydrolases


Relationship
Family|Haloalkane_dehalogenase-HLD2
Block| X
Position in NCBI Life Tree|Renilla reniformis
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Cnidaria: N E > Anthozoa: N E > Octocorallia: N E > Pennatulacea: N E > Sessiliflorae: N E > Renillidae: N E > Renilla: N E > Renilla reniformis: N E


Molecular evidence
Database
No mutation
9 structures (e.g. : 2PSD, 2PSE, 2PSF... more)
No kinetic





1 substrate:
Coelenterazine
1 inhbitor:
Coelenteramide
1 Genbank : M63501
1 UniProt : P27652
1 Ncbi-nid : 160819
1 Ncbi-pid : 160820
>3 Structure links 6 more: 6YN2, 7OMR, 7OMO
1 UniProt : P27652
1 Interpro : P27652
1 Prodom : P27652
1 Pfam : P27652
1 PIRSF : P27652
1 SUPERFAM : P27652
Sequence
Graphical view for this peptide sequence: renre-luc
Colored MSA for Haloalkane_dehalogenase-HLD2 (raw)
MTSKVYDPEQRKRMITGPQWWARCKQMNVLDSFINYYDSEKHAENAVIFL
HGNAASSYLWRHVVPHIEPVARCIIPDLIGMGKSGKSGNGSYRLLDHYKY
LTAWFELLNLPKKIIFVGHDWGACLAFHYSYEHQDKIKAIVHAESVVDVI
ESWDEWPDIEEDIALIKSEEGEKMVLENNFFVETMLPSKIMRKLEPEEFA
AYLEPFKEKGEVRRPTLSWPREIPLVKGGKPDVVQIVRNYNAYLRASDDL
PKMFIESDPGFFSNAIVEGAKKFPNTEFVKVKGLHFSQEDAPDEMGKYIK
SFVERVLKNEQ
Legend This sequence has been compared to family alignement (MSA)
red => minority aminoacid
blue => majority aminoacid
color intensity => conservation rate
title => sequence position(MSA position)aminoacid rate
Catalytic site
Catalytic site in the MSA

MTSKVYDPEQRKRMITGPQWWARCKQMNVLDSFINYYDSEKHAENAVIFL
HGNAASSYLWRHVVPHIEPVARCIIPDLIGMGKSGKSGNGSYRLLDHYKY
LTAWFELLNLPKKIIFVGHDWGACLAFHYSYEHQDKIKAIVHAESVVDVI
ESWDEWPDIEEDIALIKSEEGEKMVLENNFFVETMLPSKIMRKLEPEEFA
AYLEPFKEKGEVRRPTLSWPREIPLVKGGKPDVVQIVRNYNAYLRASDDL
PKMFIESDPGFFSNAIVEGAKKFPNTEFVKVKGLHFSQEDAPDEMGKYIK
SFVERVLKNEQ


References
5 more
    Title: A catalytic mechanism for Renilla-type bioluminescence
    Schenkmayerova A, Toul M, Pluskal D, Baatallah R, Gagnot G, Pinto GP, Santana VT, Stuchla M, Neugebauer P and Marek M <5 more author(s)>
    Ref: Biorxiv, :, 2022 : PubMed

            

    Title: Engineering the protein dynamics of an ancestral luciferase
    Schenkmayerova A, Pinto GP, Toul M, Marek M, Hernychova L, Planas-Iglesias J, Daniel Liskova V, Pluskal D, Vasina M and Damborsky J <7 more author(s)>
    Ref: Nat Commun, 12:3616, 2021 : PubMed

            

    Title: Probing the emitter site of Renilla luciferase using small organic molecules; an attempt to understand the molecular architecture of the emitter site
    Salehi F, Emamzadeh R, Nazari M, Rasa SM
    Ref: Int J Biol Macromol, 93:1253, 2016 : PubMed

            


Other Papers


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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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