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Oplophorus-luciferin 2-monooxygenase catalytic subunit (19kOLase) (EC 1.13.12.13)

 LUCI_OPLGR              Reviewed;         196 AA.
Q9GV45;
05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
27-SEP-2017, entry version 39.
RecName: Full=Oplophorus-luciferin 2-monooxygenase catalytic subunit;
AltName: Full=19kOLase;
EC=1.13.12.13;
Flags: Precursor;
Oplophorus gracilirostris (Luminous shrimp).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Malacostraca;
Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Caridea;
Oplophoroidea; Oplophoridae; Oplophorus.
NCBI_TaxID=727944;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CATALYTIC
ACTIVITY, FUNCTION, AND SUBUNIT.
PubMed=10984608; DOI=10.1016/S0014-5793(00)01963-3;
Inouye S., Watanabe K., Nakamura H., Shimomura O.;
"Secretional luciferase of the luminous shrimp Oplophorus
gracilirostris: cDNA cloning of a novel imidazopyrazinone
luciferase(1).";
FEBS Lett. 481:19-25(2000).
[2]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=629957; DOI=10.1021/bi00599a008;
Shimomura O., Masugi T., Johnson F.H., Haneda Y.;
"Properties and reaction mechanism of the bioluminescence system of
the deep-sea shrimp Oplophorus gracilorostris.";
Biochemistry 17:994-998(1978).
[3]
CATALYTIC ACTIVITY, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=17900925; DOI=10.1016/j.pep.2007.08.002;
Inouye S., Sasaki S.;
"Overexpression, purification and characterization of the catalytic
component of Oplophorus luciferase in the deep-sea shrimp, Oplophorus
gracilirostris.";
Protein Expr. Purif. 56:261-268(2007).
-!- FUNCTION: Catalytic subunit of oplophorus-luciferin 2-
monooxygenase. Oxidoreductase that converts coelenterazine (the
oplophorus luciferin) to coelenteramide under emission of blue
light with a maximum at 454 nm. Is also active with
bisdeoxycoelenterazine. {ECO:0000269|PubMed:10984608}.
-!- CATALYTIC ACTIVITY: Oplophorus luciferin + O(2) = oxidized
Oplophorus luciferin + CO(2) + light.
{ECO:0000269|PubMed:10984608, ECO:0000269|PubMed:17900925,
ECO:0000269|PubMed:629957}.
-!- ENZYME REGULATION: Inhibited by micromolar Cu(2+).
{ECO:0000269|PubMed:17900925}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.73 uM for coelenterazine {ECO:0000269|PubMed:17900925,
ECO:0000269|PubMed:629957};
KM=1.3 uM for bis-coelenterazine {ECO:0000269|PubMed:17900925,
ECO:0000269|PubMed:629957};
pH dependence:
Optimum pH is 8-9. {ECO:0000269|PubMed:17900925,
ECO:0000269|PubMed:629957};
Temperature dependence:
Optimum temperature is 40 degrees Celsius.
{ECO:0000269|PubMed:17900925, ECO:0000269|PubMed:629957};
-!- SUBUNIT: Heterotetramer of a catalytic 19 kDa and a non-catalytic
35 kDa subunit. {ECO:0000269|PubMed:10984608}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
-!- MISCELLANEOUS: The shrimp has luminous glands at the base of its
antennae and legs, and ejects a cloud of brightly luminescent
secretion from the base of its antennae upon stimulation.
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EMBL; AB030246; BAB13776.1; -; mRNA.
PDB; 5B0U; X-ray; 1.71 A; A/B=28-196.
PDB; 5IBO; X-ray; 1.95 A; A/B=28-196.
PDBsum; 5B0U; -.
PDBsum; 5IBO; -.
SMR; Q9GV45; -.
BindingDB; Q9GV45; -.
KEGG; ag:BAB13776; -.
KO; K21823; -.
BRENDA; 1.13.12.13; 4421.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0033756; F:Oplophorus-luciferin 2-monooxygenase activity; IDA:UniProtKB.
GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
InterPro; IPR012674; Calycin.
SUPFAM; SSF50814; SSF50814; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Luminescence; Oxidoreductase;
Secreted; Signal.
SIGNAL 1 27 {ECO:0000305}.
CHAIN 28 196 Oplophorus-luciferin 2-monooxygenase
catalytic subunit.
/FTId=PRO_0000418820.
HELIX 30 33 {ECO:0000244|PDB:5B0U}.
STRAND 35 44 {ECO:0000244|PDB:5B0U}.
HELIX 45 51 {ECO:0000244|PDB:5B0U}.
HELIX 57 61 {ECO:0000244|PDB:5B0U}.
STRAND 66 74 {ECO:0000244|PDB:5B0U}.
TURN 75 77 {ECO:0000244|PDB:5B0U}.
STRAND 78 89 {ECO:0000244|PDB:5B0U}.
HELIX 94 104 {ECO:0000244|PDB:5B0U}.
STRAND 111 125 {ECO:0000244|PDB:5B0U}.
STRAND 127 130 {ECO:0000244|PDB:5B0U}.
STRAND 132 134 {ECO:0000244|PDB:5B0U}.
STRAND 141 147 {ECO:0000244|PDB:5B0U}.
STRAND 149 157 {ECO:0000244|PDB:5B0U}.
STRAND 163 170 {ECO:0000244|PDB:5B0U}.
STRAND 176 182 {ECO:0000244|PDB:5B0U}.
STRAND 185 193 {ECO:0000244|PDB:5B0U}.
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


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