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P27652

- LUCI_RENRE

UniProt

P27652 - LUCI_RENRE

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Protein
Renilla-luciferin 2-monooxygenase
Gene
N/A
Organism
Renilla reniformis (Sea pansy)
Status
Reviewed - 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. Renilla-luciferin 2-monooxygenase activity Source: UniProtKB-EC
  2. carboxy-lyase activity Source: UniProtKB-KW

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.

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-monooxygenase
PRO_0000084523Add
BLAST

Interactioni

Subunit structurei

Monomer.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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

MTSKVYDPEQ RKRMITGPQW WARCKQMNVL DSFINYYDSE KHAENAVIFL    50
HGNAASSYLW RHVVPHIEPV ARCIIPDLIG MGKSGKSGNG SYRLLDHYKY 100
LTAWFELLNL PKKIIFVGHD WGACLAFHYS YEHQDKIKAI VHAESVVDVI 150
ESWDEWPDIE EDIALIKSEE GEKMVLENNF FVETMLPSKI MRKLEPEEFA 200
AYLEPFKEKG EVRRPTLSWP REIPLVKGGK PDVVQIVRNY NAYLRASDDL 250
PKMFIESDPG FFSNAIVEGA KKFPNTEFVK VKGLHFSQED APDEMGKYIK 300
SFVERVLKNE Q 311
Length:311
Mass (Da):36,022
Last modified:August 1, 1992 - v1
Checksum:i0A3FD025B4EC33FD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti219 – 2191W → L AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63501 mRNA. Translation: AAA29804.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M63501 mRNA. Translation: AAA29804.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2PSD X-ray 1.40 A 3-311 [» ]
2PSE X-ray 2.50 A 3-311 [» ]
2PSF X-ray 1.40 A/B 3-311 [» ]
2PSH X-ray 1.79 A/B 1-311 [» ]
2PSJ X-ray 1.80 A/B 1-311 [» ]
ProteinModelPortali P27652.
SMRi P27652. Positions 3-309.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2303641.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16919.

Miscellaneous databases

EvolutionaryTracei P27652.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view ]
Pfami PF00561. Abhydrolase_1. 1 hit.
[Graphical view ]
PRINTSi PR00412. EPOXHYDRLASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

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: July 9, 2014
This is version 64 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

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