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Protein

Coelenterazine h 2-monooxygenase

Gene
N/A
Organism
Renilla reniformis (Sea pansy)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Upon binding the substrate, the enzyme catalyzes an oxygenation, producing a very short-lived hydroperoxide that cyclizes into a dioxetanone structure, which collapses, releasing a CO2 molecule. The spontaneous breakdown of the dioxetanone releases the energy (about 50 kcal/mole) that is necessary to generate the excited state of the coelenteramide product, which is the singlet form of the monoanion. In vivo the product undergoes the process of nonradiative energy transfer to an accessory protein, a green fluorescent protein (GFP), which results in green bioluminescence. In vitro, in the absence of GFP, the product emits blue light.1 Publication

Miscellaneous

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.

Catalytic activityi

Coelenterazine h + O2 = excited coelenteramide h monoanion + CO2.1 Publication

pH dependencei

Optimum pH is 7.4.1 Publication

Temperature dependencei

Optimum temperature is 32 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei162SubstrateCombined sources1
Binding sitei285SubstrateCombined sources1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDecarboxylase, Lyase, Monooxygenase, Oxidoreductase, Photoprotein
Biological processLuminescence

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16919
BRENDAi1.13.12.5 5324

Protein family/group databases

ESTHERirenre-luc Haloalkane_dehalogenase-HLD2

Names & Taxonomyi

Protein namesi
Recommended name:
Coelenterazine h 2-monooxygenase (EC:1.13.12.51 Publication)
Alternative name(s):
Renilla-luciferin 2-monooxygenase
Renilla-type luciferase
OrganismiRenilla reniformis (Sea pansy)
Taxonomic identifieri6136 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaOctocoralliaPennatulaceaSessilifloraeRenillidaeRenilla

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2303641

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000845231 – 311Coelenterazine h 2-monooxygenaseAdd BLAST311

Proteomic databases

PRIDEiP27652

Interactioni

Subunit structurei

Monomer.2 Publications

Structurei

Secondary structure

1311
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 13Combined sources4
Helixi17 – 23Combined sources7
Beta strandi25 – 29Combined sources5
Beta strandi32 – 38Combined sources7
Beta strandi45 – 50Combined sources6
Helixi57 – 60Combined sources4
Turni61 – 63Combined sources3
Helixi64 – 66Combined sources3
Turni67 – 70Combined sources4
Beta strandi71 – 76Combined sources6
Helixi94 – 105Combined sources12
Turni106 – 109Combined sources4
Beta strandi112 – 119Combined sources8
Helixi121 – 132Combined sources12
Beta strandi136 – 144Combined sources9
Helixi160 – 167Combined sources8
Helixi170 – 175Combined sources6
Turni176 – 178Combined sources3
Helixi180 – 183Combined sources4
Helixi185 – 188Combined sources4
Beta strandi191 – 193Combined sources3
Helixi196 – 203Combined sources8
Helixi204 – 206Combined sources3
Beta strandi208 – 210Combined sources3
Helixi211 – 213Combined sources3
Helixi214 – 221Combined sources8
Turni226 – 228Combined sources3
Helixi231 – 245Combined sources15
Beta strandi252 – 259Combined sources8
Helixi263 – 270Combined sources8
Beta strandi273 – 286Combined sources14
Helixi287 – 289Combined sources3
Helixi292 – 307Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2PSDX-ray1.40A3-311[»]
2PSEX-ray2.50A3-311[»]
2PSFX-ray1.40A/B3-311[»]
2PSHX-ray1.79A/B1-311[»]
2PSJX-ray1.80A/B1-311[»]
ProteinModelPortaliP27652
SMRiP27652
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27652

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 291AB hydrolase-1Sequence analysisAdd BLAST247

Phylogenomic databases

KOiK18053

Family and domain databases

Gene3Di3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000073 AB_hydrolase_1
IPR000639 Epox_hydrolase-like
PfamiView protein in Pfam
PF00561 Abhydrolase_1, 1 hit
PRINTSiPR00412 EPOXHYDRLASE
SUPFAMiSSF53474 SSF53474, 1 hit

Sequencei

Sequence statusi: Complete.

P27652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSKVYDPEQ RKRMITGPQW WARCKQMNVL DSFINYYDSE KHAENAVIFL
60 70 80 90 100
HGNAASSYLW RHVVPHIEPV ARCIIPDLIG MGKSGKSGNG SYRLLDHYKY
110 120 130 140 150
LTAWFELLNL PKKIIFVGHD WGACLAFHYS YEHQDKIKAI VHAESVVDVI
160 170 180 190 200
ESWDEWPDIE EDIALIKSEE GEKMVLENNF FVETMLPSKI MRKLEPEEFA
210 220 230 240 250
AYLEPFKEKG EVRRPTLSWP REIPLVKGGK PDVVQIVRNY NAYLRASDDL
260 270 280 290 300
PKMFIESDPG FFSNAIVEGA KKFPNTEFVK VKGLHFSQED APDEMGKYIK
310
SFVERVLKNE Q
Length:311
Mass (Da):36,022
Last modified:August 1, 1992 - v1
Checksum:i0A3FD025B4EC33FD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti219W → L AA sequence (PubMed:1674607).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63501 mRNA Translation: AAA29804.1

Genome annotation databases

KEGGiag:AAA29804

Similar proteinsi

Entry informationi

Entry nameiLUCI_RENRE
AccessioniPrimary (citable) accession number: P27652
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: May 23, 2018
This is version 76 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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