ID LUCI_PHOPY Reviewed; 550 AA. AC P08659; Q27755; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 26-NOV-2014, entry version 97. DE RecName: Full=Luciferin 4-monooxygenase; DE Short=Luciferase; DE EC=1.13.12.7; OS Photinus pyralis (Common eastern firefly) (Lampyris pyralis). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Coleoptera; Polyphaga; OC Elateriformia; Elateroidea; Lampyridae; Lampyrinae; Photinus. OX NCBI_TaxID=7054; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3821727; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Croizier G.M.J.; RT "Construction and utilization of an Autographa californica nuclear RT polyhedrosis virus vector with a unique cloning site: expression of RT genes amplified by the polymerase chain reaction."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SUBCELLULAR LOCATION. RX PubMed=3554235; DOI=10.1073/pnas.84.10.3264; 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 [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=8805533; DOI=10.1016/S0969-2126(96)00033-0; RA Conti E., Franks N.P., Brick P.; RT "Crystal structure of firefly luciferase throws light on a superfamily RT of adenylate-forming enzymes."; RL Structure 4:287-298(1996). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=9788915; DOI=10.1016/S0006-3495(98)77664-7; 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: Photinus luciferin + O(2) + ATP = oxidized CC Photinus luciferin + CO(2) + AMP + diphosphate + light. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:3554235}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Firefly luciferase entry; CC URL="http://en.wikipedia.org/wiki/Firefly_luciferase"; 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; -; Genomic_DNA. DR EMBL; X84846; CAA59281.1; -; Genomic_DNA. DR EMBL; X84848; CAA59283.1; -; Genomic_DNA. DR EMBL; U03687; AAA03561.1; -; Unassigned_DNA. DR EMBL; U89934; AAB64396.1; -; Genomic_DNA. DR EMBL; U89935; AAB64399.1; -; Genomic_DNA. DR PIR; A26772; A26772. DR PDB; 1BA3; X-ray; 2.20 A; A=1-550. DR PDB; 1LCI; X-ray; 2.00 A; A=1-550. DR PDB; 3IEP; X-ray; 2.10 A; A=1-550. DR PDB; 3IER; X-ray; 2.05 A; A=1-550. DR PDB; 3IES; X-ray; 2.00 A; A=1-550. DR PDB; 3RIX; X-ray; 1.70 A; A=1-550. DR PDB; 4E5D; X-ray; 2.20 A; A=1-550. DR PDB; 4G36; X-ray; 2.62 A; A/B=1-550. DR PDB; 4G37; X-ray; 2.40 A; A/B=1-550. DR PDBsum; 1BA3; -. DR PDBsum; 1LCI; -. DR PDBsum; 3IEP; -. DR PDBsum; 3IER; -. DR PDBsum; 3IES; -. DR PDBsum; 3RIX; -. DR PDBsum; 4E5D; -. DR PDBsum; 4G36; -. DR PDBsum; 4G37; -. DR ProteinModelPortal; P08659; -. DR SMR; P08659; 3-544. DR IntAct; P08659; 1. DR MINT; MINT-7890251; -. DR BindingDB; P08659; -. DR ChEMBL; CHEMBL5567; -. DR BioCyc; MetaCyc:MONOMER-16917; -. DR SABIO-RK; P08659; -. DR EvolutionaryTrace; P08659; -. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0047077; F:Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC. DR GO; GO:0008218; P:bioluminescence; IEA:UniProtKB-KW. DR Gene3D; 4.10.8.10; -; 1. DR InterPro; IPR025110; AMP-bd_C. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR InterPro; IPR027380; Luciferase_N_dom. DR Pfam; PF00501; AMP-binding; 1. DR Pfam; PF13193; AMP-binding_C; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Luminescence; Magnesium; Metal-binding; KW Monooxygenase; Nucleotide-binding; Oxidoreductase; Peroxisome; KW Photoprotein. FT CHAIN 1 550 Luciferin 4-monooxygenase. FT /FTId=PRO_0000193147. FT MOTIF 548 550 Microbody targeting signal. FT CONFLICT 361 361 A -> G (in Ref. 2; CAA59281). FT {ECO:0000305}. FT HELIX 4 6 {ECO:0000244|PDB:3RIX}. FT STRAND 7 9 {ECO:0000244|PDB:3RIX}. FT HELIX 22 34 {ECO:0000244|PDB:3RIX}. FT STRAND 40 44 {ECO:0000244|PDB:3RIX}. FT TURN 45 47 {ECO:0000244|PDB:3RIX}. FT STRAND 50 52 {ECO:0000244|PDB:3RIX}. FT HELIX 53 70 {ECO:0000244|PDB:3RIX}. FT STRAND 77 81 {ECO:0000244|PDB:3RIX}. FT TURN 86 88 {ECO:0000244|PDB:3RIX}. FT HELIX 89 97 {ECO:0000244|PDB:3RIX}. FT STRAND 101 104 {ECO:0000244|PDB:3RIX}. FT HELIX 111 121 {ECO:0000244|PDB:3RIX}. FT STRAND 124 128 {ECO:0000244|PDB:3RIX}. FT HELIX 130 132 {ECO:0000244|PDB:3RIX}. FT HELIX 133 142 {ECO:0000244|PDB:3RIX}. FT STRAND 148 151 {ECO:0000244|PDB:3RIX}. FT STRAND 161 163 {ECO:0000244|PDB:1LCI}. FT HELIX 164 171 {ECO:0000244|PDB:3RIX}. FT TURN 178 180 {ECO:0000244|PDB:3RIX}. FT TURN 188 190 {ECO:0000244|PDB:3RIX}. FT STRAND 191 197 {ECO:0000244|PDB:3RIX}. FT STRAND 207 211 {ECO:0000244|PDB:3RIX}. FT HELIX 212 222 {ECO:0000244|PDB:3RIX}. FT TURN 225 227 {ECO:0000244|PDB:3RIX}. FT STRAND 236 239 {ECO:0000244|PDB:3RIX}. FT HELIX 246 258 {ECO:0000244|PDB:3RIX}. FT STRAND 261 264 {ECO:0000244|PDB:3RIX}. FT HELIX 270 279 {ECO:0000244|PDB:3RIX}. FT STRAND 283 287 {ECO:0000244|PDB:3RIX}. FT HELIX 289 297 {ECO:0000244|PDB:3RIX}. FT HELIX 300 303 {ECO:0000244|PDB:3RIX}. FT STRAND 311 314 {ECO:0000244|PDB:3RIX}. FT HELIX 321 330 {ECO:0000244|PDB:3RIX}. FT STRAND 337 341 {ECO:0000244|PDB:3RIX}. FT HELIX 343 345 {ECO:0000244|PDB:3RIX}. FT STRAND 346 351 {ECO:0000244|PDB:3RIX}. FT STRAND 363 365 {ECO:0000244|PDB:3RIX}. FT STRAND 370 374 {ECO:0000244|PDB:3RIX}. FT TURN 376 378 {ECO:0000244|PDB:3RIX}. FT STRAND 388 394 {ECO:0000244|PDB:3RIX}. FT STRAND 399 401 {ECO:0000244|PDB:3RIX}. FT HELIX 405 411 {ECO:0000244|PDB:3RIX}. FT STRAND 418 426 {ECO:0000244|PDB:3RIX}. FT STRAND 432 434 {ECO:0000244|PDB:3RIX}. FT HELIX 437 439 {ECO:0000244|PDB:1BA3}. FT STRAND 442 444 {ECO:0000244|PDB:1LCI}. FT STRAND 447 449 {ECO:0000244|PDB:1LCI}. FT HELIX 451 459 {ECO:0000244|PDB:1LCI}. FT STRAND 464 474 {ECO:0000244|PDB:1LCI}. FT TURN 475 477 {ECO:0000244|PDB:1LCI}. FT STRAND 478 487 {ECO:0000244|PDB:1LCI}. FT HELIX 495 505 {ECO:0000244|PDB:1LCI}. FT HELIX 508 510 {ECO:0000244|PDB:1LCI}. FT STRAND 515 521 {ECO:0000244|PDB:1LCI}. FT STRAND 528 530 {ECO:0000244|PDB:1BA3}. FT HELIX 532 542 {ECO:0000244|PDB:1LCI}. 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 //