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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

GO - Biological processi

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.

Protein family/group databases

ESTHERirenre-luc. Haloalkane_dehalogenase-HLD2.

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

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2303641.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000845231 – 311Renilla-luciferin 2-monooxygenaseAdd BLAST311

Interactioni

Subunit structurei

Monomer.

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

Sequence similaritiesi

Phylogenomic databases

KOiK18053.

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)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.

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
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...

Chemistry databases

ChEMBLiCHEMBL2303641.

Protein family/group databases

ESTHERirenre-luc. Haloalkane_dehalogenase-HLD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAA29804.

Phylogenomic databases

KOiK18053.

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...

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: November 2, 2016
This is version 73 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
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.