LUCI_PHOPY
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 25-MAY-2022, entry version 128.
DE RecName: Full=Luciferin 4-monooxygenase;
DE Short=Luciferase;
DE EC=1.13.12.7 {ECO:0000250|UniProtKB:Q26304};
OS Photinus pyralis (Common eastern firefly) (Lampyris pyralis).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea;
OC Lampyridae; Lampyrinae; Photinus.
OX NCBI_TaxID=7054;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3821727; DOI=10.1128/mcb.7.2.725-737.1987;
RA de Wet J.R., Wood K.V., Deluca M., Helinski D.R., Subramani S.;
RT "Firefly luciferase gene: structure and expression in mammalian 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 genes
RT 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 of
RT 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 general
RT anesthetic.";
RL Biophys. J. 75:2205-2211(1998).
CC -!- FUNCTION: Produces green light with a wavelength of 562 nm.
CC {ECO:0000250|UniProtKB:Q26304}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + firefly D-luciferin + O2 = AMP + CO2 + diphosphate +
CC firefly oxyluciferin + hnu; Xref=Rhea:RHEA:10732, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16792, ChEBI:CHEBI:30212,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58038,
CC ChEBI:CHEBI:456215; EC=1.13.12.7;
CC Evidence={ECO:0000250|UniProtKB:Q26304};
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 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Firefly luciferase entry;
CC URL="https://en.wikipedia.org/wiki/Firefly_luciferase";
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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 PDB; 5DV9; X-ray; 2.40 A; A=1-550.
DR PDB; 5DWV; X-ray; 2.30 A; A=1-550.
DR PDB; 5GYZ; X-ray; 2.40 A; A=4-438.
DR PDB; 5GZ2; X-ray; 2.00 A; A=3-438.
DR PDB; 5KYT; X-ray; 2.00 A; A/B=1-550.
DR PDB; 5KYV; X-ray; 2.50 A; A/B=1-550.
DR PDB; 5WYS; X-ray; 3.00 A; A=1-550.
DR PDB; 6HPS; X-ray; 3.10 A; A/B=4-546.
DR PDB; 6Q2M; X-ray; 2.75 A; A/B/C=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 PDBsum; 5DV9; -.
DR PDBsum; 5DWV; -.
DR PDBsum; 5GYZ; -.
DR PDBsum; 5GZ2; -.
DR PDBsum; 5KYT; -.
DR PDBsum; 5KYV; -.
DR PDBsum; 5WYS; -.
DR PDBsum; 6HPS; -.
DR PDBsum; 6Q2M; -.
DR AlphaFoldDB; P08659; -.
DR BMRB; P08659; -.
DR SMR; P08659; -.
DR ELM; P08659; -.
DR IntAct; P08659; 1.
DR MINT; P08659; -.
DR BindingDB; P08659; -.
DR ChEMBL; CHEMBL5567; -.
DR BRENDA; 1.13.12.7; 4775.
DR BRENDA; 6.2.1.3; 4775.
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:0051087; F:chaperone binding; IPI:CAFA.
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; 3.30.300.30; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
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
FT /note="Luciferin 4-monooxygenase"
FT /id="PRO_0000193147"
FT MOTIF 548..550
FT /note="Microbody targeting signal"
FT CONFLICT 361
FT /note="A -> G (in Ref. 2; CAA59281)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 22..34
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:3RIX"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 53..70
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3RIX"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 124..128
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1LCI"
FT HELIX 164..171
FT /evidence="ECO:0007829|PDB:3RIX"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3RIX"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:5KYT"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:3RIX"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 270..279
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 300..303
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:3RIX"
FT TURN 376..378
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 388..394
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:3RIX"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:5WYS"
FT STRAND 418..426
FT /evidence="ECO:0007829|PDB:3RIX"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:3RIX"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:5KYT"
FT STRAND 442..444
FT /evidence="ECO:0007829|PDB:1LCI"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:1LCI"
FT HELIX 451..459
FT /evidence="ECO:0007829|PDB:1LCI"
FT STRAND 464..474
FT /evidence="ECO:0007829|PDB:1LCI"
FT TURN 475..477
FT /evidence="ECO:0007829|PDB:1LCI"
FT STRAND 478..487
FT /evidence="ECO:0007829|PDB:1LCI"
FT HELIX 495..505
FT /evidence="ECO:0007829|PDB:1LCI"
FT HELIX 508..510
FT /evidence="ECO:0007829|PDB:1LCI"
FT STRAND 515..521
FT /evidence="ECO:0007829|PDB:1LCI"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:1BA3"
FT HELIX 532..542
FT /evidence="ECO:0007829|PDB:1LCI"
FT TURN 544..546
FT /evidence="ECO:0007829|PDB:4G36"
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
