ID LUCI_RENRE Reviewed; 311 AA. AC P27652; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=Coelenterazine h 2-monooxygenase; DE EC=1.13.12.5 {ECO:0000269|PubMed:1674607}; DE AltName: Full=Renilla-luciferin 2-monooxygenase; DE AltName: Full=Renilla-type luciferase; OS Renilla reniformis (Sea pansy). OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Octocorallia; Scleralcyonacea; OC Pennatuloidea; Sessiliflorae; Renillidae; Renilla. OX NCBI_TaxID=6136; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 161-183; 208-228; 256-277 RP AND 304-310, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=1674607; DOI=10.1073/pnas.88.10.4438; RA Lorenz W.W., McCann R.O., Longiaru M., Cormier M.J.; RT "Isolation and expression of a cDNA encoding Renilla reniformis RT luciferase."; RL Proc. Natl. Acad. Sci. U.S.A. 88:4438-4442(1991). RN [2] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=12797; DOI=10.1021/bi00620a014; RA Matthews J.C., Hori K., Cormier M.J.; RT "Purification and properties of Renilla reniformis luciferase."; RL Biochemistry 16:85-91(1977). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 3-311 OF APOENZYME AND IN COMPLEX RP WITH COELENTERAMIDE H, AND SUBUNIT. RX PubMed=17980388; DOI=10.1016/j.jmb.2007.09.078; RA Loening A.M., Fenn T.D., Gambhir S.S.; RT "Crystal structures of the luciferase and green fluorescent protein from RT Renilla reniformis."; RL J. Mol. Biol. 374:1017-1028(2007). CC -!- FUNCTION: Upon binding the substrate, the enzyme catalyzes an CC oxygenation, producing a very short-lived hydroperoxide that cyclizes CC into a dioxetanone structure, which collapses, releasing a CO(2) CC molecule. The spontaneous breakdown of the dioxetanone releases the CC energy (about 50 kcal/mole) that is necessary to generate the excited CC state of the coelenteramide product, which is the singlet form of the CC monoanion. In vivo the product undergoes the process of nonradiative CC energy transfer to an accessory protein, a green fluorescent protein CC (GFP), which results in green bioluminescence. In vitro, in the absence CC of GFP, the product emits blue light. {ECO:0000269|PubMed:1674607}. CC -!- CATALYTIC ACTIVITY: CC Reaction=coelenterazine h + O2 = CO2 + excited coelenteramide h CC monoanion + H(+) + hnu; Xref=Rhea:RHEA:14765, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16531, CC ChEBI:CHEBI:30212, ChEBI:CHEBI:138275; EC=1.13.12.5; CC Evidence={ECO:0000269|PubMed:1674607}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.4. {ECO:0000269|PubMed:12797}; CC Temperature dependence: CC Optimum temperature is 32 degrees Celsius. CC {ECO:0000269|PubMed:12797}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12797, CC ECO:0000269|PubMed:17980388}. CC -!- MISCELLANEOUS: This luciferase produces light with a wavelength of 480 CC nm. In presence of a green fluorescence protein (GFP) it produces a CC green fluorescence at 509 nm. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M63501; AAA29804.1; -; mRNA. DR PDB; 2PSD; X-ray; 1.40 A; A=3-311. DR PDB; 2PSE; X-ray; 2.50 A; A=3-311. DR PDB; 2PSF; X-ray; 1.40 A; A/B=3-311. DR PDB; 2PSH; X-ray; 1.79 A; A/B=1-311. DR PDB; 2PSJ; X-ray; 1.80 A; A/B=1-311. DR PDB; 6YN2; X-ray; 1.90 A; A/B=1-311. DR PDB; 7OMD; X-ray; 1.60 A; A/B=1-311. DR PDB; 7OMO; X-ray; 1.45 A; A/B=1-311. DR PDB; 7OMR; X-ray; 1.50 A; A=1-311. DR PDBsum; 2PSD; -. DR PDBsum; 2PSE; -. DR PDBsum; 2PSF; -. DR PDBsum; 2PSH; -. DR PDBsum; 2PSJ; -. DR PDBsum; 6YN2; -. DR PDBsum; 7OMD; -. DR PDBsum; 7OMO; -. DR PDBsum; 7OMR; -. DR AlphaFoldDB; P27652; -. DR SMR; P27652; -. DR ChEMBL; CHEMBL2303641; -. DR ESTHER; renre-luc; Haloalkane_dehalogenase-HLD2. DR KEGG; ag:AAA29804; -. DR BioCyc; MetaCyc:MONOMER-16919; -. DR BRENDA; 1.13.12.5; 5324. DR EvolutionaryTrace; P27652; -. DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW. DR GO; GO:0050248; F:Renilla-luciferin 2-monooxygenase activity; IEA:UniProtKB-EC. DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR000639; Epox_hydrolase-like. DR PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1. DR PANTHER; PTHR43329:SF74; HALOALKANE DEHALOGENASE; 1. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00412; EPOXHYDRLASE. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. PE 1: Evidence at protein level; KW 3D-structure; Decarboxylase; Direct protein sequencing; Luminescence; KW Lyase; Monooxygenase; Oxidoreductase; Photoprotein. FT CHAIN 1..311 FT /note="Coelenterazine h 2-monooxygenase" FT /id="PRO_0000084523" FT DOMAIN 45..291 FT /note="AB hydrolase-1" FT /evidence="ECO:0000255" FT BINDING 162 FT /ligand="substrate" FT /evidence="ECO:0007744|PDB:2PSJ" FT BINDING 285 FT /ligand="substrate" FT /evidence="ECO:0007744|PDB:2PSJ" FT CONFLICT 219 FT /note="W -> L (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 10..13 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 17..23 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 25..29 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 32..38 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:2PSD" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:2PSD" FT TURN 67..70 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 71..76 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 88..90 FT /evidence="ECO:0007829|PDB:7OMD" FT HELIX 94..105 FT /evidence="ECO:0007829|PDB:2PSD" FT TURN 106..109 FT /evidence="ECO:0007829|PDB:2PSF" FT STRAND 112..119 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 121..132 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 136..144 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 152..154 FT /evidence="ECO:0007829|PDB:7OMR" FT HELIX 160..167 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 170..175 FT /evidence="ECO:0007829|PDB:2PSD" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 180..183 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 185..188 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 191..193 FT /evidence="ECO:0007829|PDB:7OMR" FT HELIX 196..203 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 204..206 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 211..213 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 214..221 FT /evidence="ECO:0007829|PDB:2PSD" FT TURN 226..228 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 231..245 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 252..259 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 263..270 FT /evidence="ECO:0007829|PDB:2PSD" FT STRAND 273..286 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:2PSD" FT HELIX 292..307 FT /evidence="ECO:0007829|PDB:2PSD" SQ 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 //