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Protein

Renilla-luciferin 2-monooxygenase

Gene
N/A
Organism
Renilla reniformis (Sea pansy)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Renilla luciferin + O2 = oxidized Renilla luciferin + CO2 + light.

GO - Molecular functioni

  1. carboxy-lyase activity Source: UniProtKB-KW
  2. Renilla-luciferin 2-monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. bioluminescence Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Decarboxylase, Lyase, Monooxygenase, Oxidoreductase, Photoprotein

Keywords - Biological processi

Luminescence

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16919.
BRENDAi1.13.12.5. 5324.

Names & Taxonomyi

Protein namesi
Recommended name:
Renilla-luciferin 2-monooxygenase (EC:1.13.12.5)
Alternative name(s):
Renilla-type luciferase
OrganismiRenilla reniformis (Sea pansy)
Taxonomic identifieri6136 [NCBI]
Taxonomic lineageiEukaryotaMetazoaCnidariaAnthozoaOctocoralliaPennatulaceaSessilifloraeRenillidaeRenilla

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 311311Renilla-luciferin 2-monooxygenasePRO_0000084523Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

1
311
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 134Combined sources
Helixi17 – 237Combined sources
Beta strandi25 – 295Combined sources
Beta strandi32 – 387Combined sources
Beta strandi45 – 506Combined sources
Helixi57 – 604Combined sources
Turni61 – 633Combined sources
Helixi64 – 663Combined sources
Turni67 – 704Combined sources
Beta strandi71 – 766Combined sources
Helixi94 – 10512Combined sources
Turni106 – 1094Combined sources
Beta strandi112 – 1198Combined sources
Helixi121 – 13212Combined sources
Beta strandi136 – 1449Combined sources
Helixi160 – 1678Combined sources
Helixi170 – 1756Combined sources
Turni176 – 1783Combined sources
Helixi180 – 1834Combined sources
Helixi185 – 1884Combined sources
Beta strandi191 – 1933Combined sources
Helixi196 – 2038Combined sources
Helixi204 – 2063Combined sources
Beta strandi208 – 2103Combined sources
Helixi211 – 2133Combined sources
Helixi214 – 2218Combined sources
Turni226 – 2283Combined sources
Helixi231 – 24515Combined sources
Beta strandi252 – 2598Combined sources
Helixi263 – 2708Combined sources
Beta strandi273 – 28614Combined sources
Helixi287 – 2893Combined sources
Helixi292 – 30716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-309.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27652.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti219 – 2191W → L AA sequence (PubMed:1674607).Curated

Sequence databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-309.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

ChEMBLiCHEMBL2303641.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16919.
BRENDAi1.13.12.5. 5324.

Miscellaneous databases

EvolutionaryTraceiP27652.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Isolation and expression of a cDNA encoding Renilla reniformis luciferase."
    Lorenz W.W., McCann R.O., Longiaru M., Cormier M.J.
    Proc. Natl. Acad. Sci. U.S.A. 88:4438-4442(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiLUCI_RENRE
AccessioniPrimary (citable) accession number: P27652
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 1, 2015
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.