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Coelenterazine h 2-monooxygenase (EC 1.13.12.5) (Renilla-luciferin 2-monooxygenase) (Renilla-type luciferase)

 LUCI_RENRE              Reviewed;         311 AA.
P27652;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
25-OCT-2017, entry version 75.
RecName: Full=Coelenterazine h 2-monooxygenase;
EC=1.13.12.5 {ECO:0000269|PubMed:1674607};
AltName: Full=Renilla-luciferin 2-monooxygenase;
AltName: Full=Renilla-type luciferase;
Renilla reniformis (Sea pansy).
Eukaryota; Metazoa; Cnidaria; Anthozoa; Octocorallia; Pennatulacea;
Sessiliflorae; Renillidae; Renilla.
NCBI_TaxID=6136;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 161-183; 208-228;
256-277 AND 304-310, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=1674607; DOI=10.1073/pnas.88.10.4438;
Lorenz W.W., McCann R.O., Longiaru M., Cormier M.J.;
"Isolation and expression of a cDNA encoding Renilla reniformis
luciferase.";
Proc. Natl. Acad. Sci. U.S.A. 88:4438-4442(1991).
[2]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=12797;
Matthews J.C., Hori K., Cormier M.J.;
"Purification and properties of Renilla reniformis luciferase.";
Biochemistry 16:85-91(1977).
[3]
X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 3-311 OF APOENZYME AND IN
COMPLEX WITH COELENTERAMIDE H, AND SUBUNIT.
PubMed=17980388; DOI=10.1016/j.jmb.2007.09.078;
Loening A.M., Fenn T.D., Gambhir S.S.;
"Crystal structures of the luciferase and green fluorescent protein
from Renilla reniformis.";
J. Mol. Biol. 374:1017-1028(2007).
-!- FUNCTION: Upon binding the substrate, the enzyme catalyzes an
oxygenation, producing a very short-lived hydroperoxide that
cyclizes into a dioxetanone structure, which collapses, releasing
a CO(2) molecule. The spontaneous breakdown of the dioxetanone
releases the energy (about 50 kcal/mole) that is necessary to
generate the excited state of the coelenteramide product, which is
the singlet form of the monoanion. In vivo the product undergoes
the process of nonradiative energy transfer to an accessory
protein, a green fluorescent protein (GFP), which results in green
bioluminescence. In vitro, in the absence of GFP, the product
emits blue light. {ECO:0000269|PubMed:1674607}.
-!- CATALYTIC ACTIVITY: Coelenterazine h + O(2) = excited
coelenteramide h monoanion + CO(2). {ECO:0000269|PubMed:1674607}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 7.4. {ECO:0000269|PubMed:12797};
Temperature dependence:
Optimum temperature is 32 degrees Celsius.
{ECO:0000269|PubMed:12797};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12797,
ECO:0000269|PubMed:17980388}.
-!- 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.
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EMBL; M63501; AAA29804.1; -; mRNA.
PDB; 2PSD; X-ray; 1.40 A; A=3-311.
PDB; 2PSE; X-ray; 2.50 A; A=3-311.
PDB; 2PSF; X-ray; 1.40 A; A/B=3-311.
PDB; 2PSH; X-ray; 1.79 A; A/B=1-311.
PDB; 2PSJ; X-ray; 1.80 A; A/B=1-311.
PDBsum; 2PSD; -.
PDBsum; 2PSE; -.
PDBsum; 2PSF; -.
PDBsum; 2PSH; -.
PDBsum; 2PSJ; -.
ProteinModelPortal; P27652; -.
SMR; P27652; -.
ChEMBL; CHEMBL2303641; -.
ESTHER; renre-luc; Haloalkane_dehalogenase-HLD2.
KEGG; ag:AAA29804; -.
KO; K18053; -.
BioCyc; MetaCyc:MONOMER-16919; -.
BRENDA; 1.13.12.5; 5324.
EvolutionaryTrace; P27652; -.
GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
GO; GO:0050248; F:Renilla-luciferin 2-monooxygenase activity; IEA:UniProtKB-EC.
GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000073; AB_hydrolase_1.
InterPro; IPR000639; Epox_hydrolase-like.
Pfam; PF00561; Abhydrolase_1; 1.
PRINTS; PR00412; EPOXHYDRLASE.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Decarboxylase; Direct protein sequencing; Luminescence;
Lyase; Monooxygenase; Oxidoreductase; Photoprotein.
CHAIN 1 311 Coelenterazine h 2-monooxygenase.
/FTId=PRO_0000084523.
DOMAIN 45 291 AB hydrolase-1. {ECO:0000255}.
BINDING 162 162 Substrate. {ECO:0000244|PDB:2PSJ}.
BINDING 285 285 Substrate. {ECO:0000244|PDB:2PSJ}.
CONFLICT 219 219 W -> L (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 10 13 {ECO:0000244|PDB:2PSD}.
HELIX 17 23 {ECO:0000244|PDB:2PSD}.
STRAND 25 29 {ECO:0000244|PDB:2PSD}.
STRAND 32 38 {ECO:0000244|PDB:2PSD}.
STRAND 45 50 {ECO:0000244|PDB:2PSD}.
HELIX 57 60 {ECO:0000244|PDB:2PSD}.
TURN 61 63 {ECO:0000244|PDB:2PSD}.
HELIX 64 66 {ECO:0000244|PDB:2PSD}.
TURN 67 70 {ECO:0000244|PDB:2PSD}.
STRAND 71 76 {ECO:0000244|PDB:2PSD}.
HELIX 94 105 {ECO:0000244|PDB:2PSD}.
TURN 106 109 {ECO:0000244|PDB:2PSF}.
STRAND 112 119 {ECO:0000244|PDB:2PSD}.
HELIX 121 132 {ECO:0000244|PDB:2PSD}.
STRAND 136 144 {ECO:0000244|PDB:2PSD}.
HELIX 160 167 {ECO:0000244|PDB:2PSD}.
HELIX 170 175 {ECO:0000244|PDB:2PSD}.
TURN 176 178 {ECO:0000244|PDB:2PSD}.
HELIX 180 183 {ECO:0000244|PDB:2PSD}.
HELIX 185 188 {ECO:0000244|PDB:2PSD}.
STRAND 191 193 {ECO:0000244|PDB:2PSJ}.
HELIX 196 203 {ECO:0000244|PDB:2PSD}.
HELIX 204 206 {ECO:0000244|PDB:2PSD}.
STRAND 208 210 {ECO:0000244|PDB:2PSD}.
HELIX 211 213 {ECO:0000244|PDB:2PSD}.
HELIX 214 221 {ECO:0000244|PDB:2PSD}.
TURN 226 228 {ECO:0000244|PDB:2PSD}.
HELIX 231 245 {ECO:0000244|PDB:2PSD}.
STRAND 252 259 {ECO:0000244|PDB:2PSD}.
HELIX 263 270 {ECO:0000244|PDB:2PSD}.
STRAND 273 286 {ECO:0000244|PDB:2PSD}.
HELIX 287 289 {ECO:0000244|PDB:2PSD}.
HELIX 292 307 {ECO:0000244|PDB:2PSD}.
SEQUENCE 311 AA; 36022 MW; 0A3FD025B4EC33FD CRC64;
MTSKVYDPEQ RKRMITGPQW WARCKQMNVL DSFINYYDSE KHAENAVIFL HGNAASSYLW
RHVVPHIEPV ARCIIPDLIG MGKSGKSGNG SYRLLDHYKY LTAWFELLNL PKKIIFVGHD
WGACLAFHYS YEHQDKIKAI VHAESVVDVI ESWDEWPDIE EDIALIKSEE GEKMVLENNF
FVETMLPSKI MRKLEPEEFA AYLEPFKEKG EVRRPTLSWP REIPLVKGGK PDVVQIVRNY
NAYLRASDDL PKMFIESDPG FFSNAIVEGA KKFPNTEFVK VKGLHFSQED APDEMGKYIK
SFVERVLKNE Q


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