LUCI_LUCCR
ID LUCI_LUCCR Reviewed; 548 AA.
AC P13129;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Luciferin 4-monooxygenase;
DE Short=Luciferase;
DE EC=1.13.12.7 {ECO:0000250|UniProtKB:Q26304};
OS Luciola cruciata (Japanese firefly) (Genji firefly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia; Elateroidea;
OC Lampyridae; Luciolinae; Luciola.
OX NCBI_TaxID=7051;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2473944; DOI=10.1016/0378-1119(89)90074-7;
RA Masuda T., Tatsumi H., Nakano E.;
RT "Cloning and sequence analysis of cDNA for luciferase of a Japanese
RT firefly, Luciola cruciata.";
RL Gene 77:265-270(1989).
CC -!- FUNCTION: Produces green light with a wavelength of 544 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:0000250}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; M26194; AAA29135.1; -; mRNA.
DR PIR; JS0181; JS0181.
DR PDB; 2D1Q; X-ray; 2.30 A; A=1-548.
DR PDB; 2D1R; X-ray; 1.60 A; A=1-548.
DR PDB; 2D1S; X-ray; 1.30 A; A=1-548.
DR PDB; 2D1T; X-ray; 1.45 A; A=1-548.
DR PDBsum; 2D1Q; -.
DR PDBsum; 2D1R; -.
DR PDBsum; 2D1S; -.
DR PDBsum; 2D1T; -.
DR AlphaFoldDB; P13129; -.
DR SMR; P13129; -.
DR BRENDA; 1.13.12.7; 3080.
DR EvolutionaryTrace; P13129; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
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; 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..548
FT /note="Luciferin 4-monooxygenase"
FT /id="PRO_0000193143"
FT MOTIF 546..548
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:2D1S"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 55..72
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2D1S"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 113..123
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2D1S"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 166..172
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:2D1S"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 214..224
FT /evidence="ECO:0007829|PDB:2D1S"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 248..259
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 323..332
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:2D1S"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 407..413
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:2D1Q"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:2D1Q"
FT HELIX 453..461
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 466..476
FT /evidence="ECO:0007829|PDB:2D1S"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 480..489
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 497..505
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 510..512
FT /evidence="ECO:0007829|PDB:2D1S"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:2D1S"
FT HELIX 534..542
FT /evidence="ECO:0007829|PDB:2D1S"
SQ SEQUENCE 548 AA; 60017 MW; 2052D6189E79109F CRC64;
MENMENDENI VVGPKPFYPI EEGSAGTQLR KYMERYAKLG AIAFTNAVTG VDYSYAEYLE
KSCCLGKALQ NYGLVVDGRI ALCSENCEEF FIPVIAGLFI GVGVAPTNEI YTLRELVHSL
GISKPTIVFS SKKGLDKVIT VQKTVTTIKT IVILDSKVDY RGYQCLDTFI KRNTPPGFQA
SSFKTVEVDR KEQVALIMNS SGSTGLPKGV QLTHENTVTR FSHARDPIYG NQVSPGTAVL
TVVPFHHGFG MFTTLGYLIC GFRVVMLTKF DEETFLKTLQ DYKCTSVILV PTLFAILNKS
ELLNKYDLSN LVEIASGGAP LSKEVGEAVA RRFNLPGVRQ GYGLTETTSA IIITPEGDDK
PGASGKVVPL FKAKVIDLDT KKSLGPNRRG EVCVKGPMLM KGYVNNPEAT KELIDEEGWL
HTGDIGYYDE EKHFFIVDRL KSLIKYKGYQ VPPAELESVL LQHPSIFDAG VAGVPDPVAG
ELPGAVVVLE SGKNMTEKEV MDYVASQVSN AKRLRGGVRF VDEVPKGLTG KIDGRAIREI
LKKPVAKM
