LUCI_OPLGR
ID LUCI_OPLGR Reviewed; 196 AA.
AC Q9GV45;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Oplophorus-luciferin 2-monooxygenase catalytic subunit;
DE AltName: Full=19kOLase;
DE EC=1.13.12.13;
DE Flags: Precursor;
OS Oplophorus gracilirostris (Luminous shrimp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Caridea;
OC Oplophoroidea; Oplophoridae; Oplophorus.
OX NCBI_TaxID=727944;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY,
RP FUNCTION, AND SUBUNIT.
RX PubMed=10984608; DOI=10.1016/s0014-5793(00)01963-3;
RA Inouye S., Watanabe K., Nakamura H., Shimomura O.;
RT "Secretional luciferase of the luminous shrimp Oplophorus gracilirostris:
RT cDNA cloning of a novel imidazopyrazinone luciferase(1).";
RL FEBS Lett. 481:19-25(2000).
RN [2]
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=629957; DOI=10.1021/bi00599a008;
RA Shimomura O., Masugi T., Johnson F.H., Haneda Y.;
RT "Properties and reaction mechanism of the bioluminescence system of the
RT deep-sea shrimp Oplophorus gracilorostris.";
RL Biochemistry 17:994-998(1978).
RN [3]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17900925; DOI=10.1016/j.pep.2007.08.002;
RA Inouye S., Sasaki S.;
RT "Overexpression, purification and characterization of the catalytic
RT component of Oplophorus luciferase in the deep-sea shrimp, Oplophorus
RT gracilirostris.";
RL Protein Expr. Purif. 56:261-268(2007).
CC -!- FUNCTION: Catalytic subunit of oplophorus-luciferin 2-monooxygenase.
CC Oxidoreductase that converts coelenterazine (the oplophorus luciferin)
CC to coelenteramide under emission of blue light with a maximum at 454
CC nm. Is also active with bisdeoxycoelenterazine.
CC {ECO:0000269|PubMed:10984608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coelenterazine + O2 = CO2 + coelenteramide + hnu;
CC Xref=Rhea:RHEA:20417, ChEBI:CHEBI:2311, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:30212, ChEBI:CHEBI:41487;
CC EC=1.13.12.13; Evidence={ECO:0000269|PubMed:10984608,
CC ECO:0000269|PubMed:17900925, ECO:0000269|PubMed:629957};
CC -!- ACTIVITY REGULATION: Inhibited by micromolar Cu(2+).
CC {ECO:0000269|PubMed:17900925}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.73 uM for coelenterazine {ECO:0000269|PubMed:17900925,
CC ECO:0000269|PubMed:629957};
CC KM=1.3 uM for bis-coelenterazine {ECO:0000269|PubMed:17900925,
CC ECO:0000269|PubMed:629957};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:17900925,
CC ECO:0000269|PubMed:629957};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:17900925, ECO:0000269|PubMed:629957};
CC -!- SUBUNIT: Heterotetramer of a catalytic 19 kDa and a non-catalytic 35
CC kDa subunit. {ECO:0000269|PubMed:10984608}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- MISCELLANEOUS: The shrimp has luminous glands at the base of its
CC antennae and legs, and ejects a cloud of brightly luminescent secretion
CC from the base of its antennae upon stimulation.
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DR EMBL; AB030246; BAB13776.1; -; mRNA.
DR PDB; 5B0U; X-ray; 1.71 A; A/B=28-196.
DR PDB; 5IBO; X-ray; 1.95 A; A/B=28-196.
DR PDBsum; 5B0U; -.
DR PDBsum; 5IBO; -.
DR AlphaFoldDB; Q9GV45; -.
DR SMR; Q9GV45; -.
DR BindingDB; Q9GV45; -.
DR KEGG; ag:BAB13776; -.
DR BRENDA; 1.13.12.13; 4421.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033756; F:Oplophorus-luciferin 2-monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
DR InterPro; IPR012674; Calycin.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Luminescence; Oxidoreductase;
KW Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000305"
FT CHAIN 28..196
FT /note="Oplophorus-luciferin 2-monooxygenase catalytic
FT subunit"
FT /id="PRO_0000418820"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:5B0U"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:5B0U"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:5B0U"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 78..89
FT /evidence="ECO:0007829|PDB:5B0U"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 111..125
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:5B0U"
FT STRAND 185..193
FT /evidence="ECO:0007829|PDB:5B0U"
SQ SEQUENCE 196 AA; 21533 MW; 056DC0753F0B8CCF CRC64;
MAYSTLFIIA LTAVVTQASS TQKSNLTFTL ADFVGDWQQT AGYNQDQVLE QGGLSSLFQA
LGVSVTPIQK VVLSGENGLK ADIHVIIPYE GLSGFQMGLI EMIFKVVYPV DDHHFKIILH
YGTLVIDGVT PNMIDYFGRP YPGIAVFDGK QITVTGTLWN GNKIYDERLI NPDGSLLFRV
TINGVTGWRL CENILA
