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P27652

- LUCI_RENRE

UniProt

P27652 - LUCI_RENRE

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
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    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

    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-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 – 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.
    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

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti219 – 2191W → L AA sequence (PubMed:1674607)Curated

    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: October 1, 2014
    This is version 65 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