LUCI_RENRE
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 03-AUG-2022, entry version 87.
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; Pennatulacea;
OC 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.
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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 PDBsum; 2PSD; -.
DR PDBsum; 2PSE; -.
DR PDBsum; 2PSF; -.
DR PDBsum; 2PSH; -.
DR PDBsum; 2PSJ; -.
DR PDBsum; 6YN2; -.
DR AlphaFoldDB; P27652; -.
DR SMR; P27652; -.
DR ChEMBL; CHEMBL2303641; -.
DR ESTHER; renre-luc; Haloalkane_dehalogenase-HLD2.
DR KEGG; ag:AAA29804; -.
DR BioCyc; MetaCyc:MON-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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 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 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 TURN 153..155
FT /evidence="ECO:0007829|PDB:6YN2"
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:2PSJ"
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
