ID LUCI_PHOPY STANDARD; PRT; 550 AA. AC P08659; DT 01-JAN-1988 (Rel. 06, Created) DT 01-JAN-1988 (Rel. 06, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE LUCIFERIN 4-MONOOXYGENASE (EC 1.13.12.7) (LUCIFERASE). OS Photinus pyralis (North American firefly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Coleoptera; Polyphaga; OC Elateriformia; Cantharoidea; Lampyridae; Photinus. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87144243. RA de Wet J.R., Wood K.V., Deluca M., Helinski D.R., Subramani S.; RT "Firefly luciferase gene: structure and expression in mammalian RT cells."; RL Mol. Cell. Biol. 7:725-737(1987). RN [2] RP SUBCELLULAR LOCATION. RX MEDLINE; 87204117. RA Keller G.-A., Gould S., de Luca M., Subramani S.; RT "Firefly luciferase is targeted to peroxisomes in mammalian cells."; RL Proc. Natl. Acad. Sci. U.S.A. 84:3264-3268(1987). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX MEDLINE; 96398615. RA Conti E., Franks N.P., Brick P.; RT "Crystal structure of firefly luciferase throws light on a RT superfamily of adenylate-forming enzymes."; RL Structure 4:287-298(1996). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE; 99007339. RA Franks N.P., Jenkins A., Conti E., Lieb W.R., Brick P.; RT "Structural basis for the inhibition of firefly luciferase by a RT general anesthetic."; RL Biophys. J. 75:2205-2211(1998). CC -!- FUNCTION: PRODUCES GREEN LIGHT WITH A WAVELENGTH OF 562 NM. CC -!- CATALYTIC ACTIVITY: LUCIFERIN + O(2) + ATP = OXIDIZED LUCIFERIN + CC CO(2) + H(2)O + AMP + PYROPHOSPHATE + LIGHT. CC -!- COFACTOR: REQUIRES MAGNESIUM. CC -!- SUBCELLULAR LOCATION: PEROXISOMAL. CC -!- SIMILARITY: TO OTHER ENZYMES WHICH ACT VIA AN ATP-DEPENDENT CC COVALENT BINDING OF AMP TO THEIR SUBSTRATE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; M15077; AAA29795.1; -. DR EMBL; X84848; CAA59283.1; -. DR EMBL; U03687; AAA03561.1; -. DR EMBL; U89934; AAB64396.1; -. DR EMBL; U89935; AAB64399.1; -. DR PIR; A26772; A26772. DR PDB; 1LCI; 26-MAR-97. DR PDB; 1BA3; 11-NOV-98. DR INTERPRO; IPR000873; -. DR PFAM; PF00501; AMP-binding; 1. DR PROSITE; PS00342; MICROBODIES_CTER; 1. DR PROSITE; PS00455; AMP_BINDING; 1. KW Oxidoreductase; Monooxygenase; Photoprotein; Luminescence; Magnesium; KW Peroxisome; 3D-structure. FT SITE 548 550 MICROBODY TARGETING SIGNAL. SQ SEQUENCE 550 AA; 60745 MW; E380FCE9D56ACCDE CRC64; MEDAKNIKKG PAPFYPLEDG TAGEQLHKAM KRYALVPGTI AFTDAHIEVN ITYAEYFEMS VRLAEAMKRY GLNTNHRIVV CSENSLQFFM PVLGALFIGV AVAPANDIYN ERELLNSMNI SQPTVVFVSK KGLQKILNVQ KKLPIIQKII IMDSKTDYQG FQSMYTFVTS HLPPGFNEYD FVPESFDRDK TIALIMNSSG STGLPKGVAL PHRTACVRFS HARDPIFGNQ IIPDTAILSV VPFHHGFGMF TTLGYLICGF RVVLMYRFEE ELFLRSLQDY KIQSALLVPT LFSFFAKSTL IDKYDLSNLH EIASGGAPLS KEVGEAVAKR FHLPGIRQGY GLTETTSAIL ITPEGDDKPG AVGKVVPFFE AKVVDLDTGK TLGVNQRGEL CVRGPMIMSG YVNNPEATNA LIDKDGWLHS GDIAYWDEDE HFFIVDRLKS LIKYKGYQVA PAELESILLQ HPNIFDAGVA GLPDDDAGEL PAAVVVLEHG KTMTEKEIVD YVASQVTTAK KLRGGVVFVD EVPKGLTGKL DARKIREILI KAKKGGKSKL //