Reviewed, UniProtKB/Swiss-Prot P08659 (LUCI_PHOPY)

Names and origin

Protein names	Recommended name:     Luciferin 4-monooxygenase       Short name=Luciferase     EC=1.13.12.7
Organism	Photinus pyralis (North American firefly)
Taxonomic identifier	7054 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Coleoptera › Polyphaga › Elateriformia › Elateroidea › Lampyridae › Lampyrinae › Photinus

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Produces green light with a wavelength of 562 nm.
Catalytic activity	Photinus luciferin + O2 + ATP = oxidized Photinus luciferin + CO2 + AMP + diphosphate + light.
Cofactor	Magnesium.
Subcellular location	Peroxisome Ref.3.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Luminescence
Cellular component	Peroxisome
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Monooxygenase Oxidoreductase Photoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	bioluminescence Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Ref.3 Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 550

550

Luciferin 4-monooxygenase

PRO_0000193147

Regions

Motif

548 – 550

3

Microbody targeting signal

Experimental info

Sequence conflict

361

1

A → G in CAA59281. Ref.2

Secondary structure

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550

Helix Strand Turn

Details...

Beta strand

7 – 9

3

Helix

22 – 34

13

Beta strand

40 – 44

5

Turn

45 – 47

3

Beta strand

50 – 52

3

Helix

53 – 70

18

Beta strand

77 – 81

5

Helix

89 – 98

10

Beta strand

101 – 104

4

Helix

111 – 121

11

Beta strand

124 – 128

5

Helix

130 – 132

3

Helix

133 – 142

10

Beta strand

148 – 153

6

Beta strand

161 – 163

3

Helix

164 – 171

8

Turn

178 – 180

3

Turn

188 – 190

3

Beta strand

191 – 197

7

Beta strand

207 – 211

5

Helix

212 – 222

11

Turn

225 – 227

3

Beta strand

236 – 239

4

Helix

246 – 258

13

Beta strand

261 – 264

4

Helix

270 – 279

10

Beta strand

283 – 286

4

Helix

289 – 297

9

Helix

301 – 303

3

Beta strand

311 – 313

3

Helix

321 – 330

10

Beta strand

339 – 341

3

Helix

343 – 345

3

Beta strand

346 – 351

6

Beta strand

363 – 365

3

Beta strand

370 – 374

5

Turn

376 – 378

3

Beta strand

388 – 394

7

Beta strand

399 – 401

3

Helix

405 – 411

7

Beta strand

418 – 426

9

Beta strand

432 – 434

3

Helix

437 – 439

3

Beta strand

442 – 444

3

Beta strand

447 – 449

3

Helix

451 – 459

9

Beta strand

464 – 474

11

Turn

475 – 477

3

Beta strand

478 – 487

10

Helix

495 – 503

9

Beta strand

515 – 518

4

Beta strand

528 – 530

3

Helix

532 – 542

11

Sequences

	Sequence		Length	Mass (Da)
	P08659-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: E380FCE9D56ACCDE	FASTA	550	60,745
	10 20 30 40 50 60 MEDAKNIKKG PAPFYPLEDG TAGEQLHKAM KRYALVPGTI AFTDAHIEVN ITYAEYFEMS 70 80 90 100 110 120 VRLAEAMKRY GLNTNHRIVV CSENSLQFFM PVLGALFIGV AVAPANDIYN ERELLNSMNI 130 140 150 160 170 180 SQPTVVFVSK KGLQKILNVQ KKLPIIQKII IMDSKTDYQG FQSMYTFVTS HLPPGFNEYD 190 200 210 220 230 240 FVPESFDRDK TIALIMNSSG STGLPKGVAL PHRTACVRFS HARDPIFGNQ IIPDTAILSV 250 260 270 280 290 300 VPFHHGFGMF TTLGYLICGF RVVLMYRFEE ELFLRSLQDY KIQSALLVPT LFSFFAKSTL 310 320 330 340 350 360 IDKYDLSNLH EIASGGAPLS KEVGEAVAKR FHLPGIRQGY GLTETTSAIL ITPEGDDKPG 370 380 390 400 410 420 AVGKVVPFFE AKVVDLDTGK TLGVNQRGEL CVRGPMIMSG YVNNPEATNA LIDKDGWLHS 430 440 450 460 470 480 GDIAYWDEDE HFFIVDRLKS LIKYKGYQVA PAELESILLQ HPNIFDAGVA GLPDDDAGEL 490 500 510 520 530 540 PAAVVVLEHG KTMTEKEIVD YVASQVTTAK KLRGGVVFVD EVPKGLTGKL DARKIREILI 550 KAKKGGKSKL

References

[1]	"Firefly luciferase gene: structure and expression in mammalian cells." de Wet J.R., Wood K.V., Deluca M., Helinski D.R., Subramani S. Mol. Cell. Biol. 7:725-737(1987) [PubMed: 3821727] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Construction and utilization of an Autographa californica nuclear polyhedrosis virus vector with a unique cloning site: expression of genes amplified by the polymerase chain reaction." Croizier G.M.J. Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Firefly luciferase is targeted to peroxisomes in mammalian cells." Keller G.-A., Gould S., de Luca M., Subramani S. Proc. Natl. Acad. Sci. U.S.A. 84:3264-3268(1987) [PubMed: 3554235] [Abstract] Cited for: SUBCELLULAR LOCATION.
[4]	"Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes." Conti E., Franks N.P., Brick P. Structure 4:287-298(1996) [PubMed: 8805533] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[5]	"Structural basis for the inhibition of firefly luciferase by a general anesthetic." Franks N.P., Jenkins A., Conti E., Lieb W.R., Brick P. Biophys. J. 75:2205-2211(1998) [PubMed: 9788915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Web resources

Wikipedia

Firefly luciferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15077 Genomic DNA. Translation: AAA29795.1.
X84846 Genomic DNA. Translation: CAA59281.1.
X84848 Genomic DNA. Translation: CAA59283.1.
U03687 Unassigned DNA. Translation: AAA03561.1.
U89934 Genomic DNA. Translation: AAB64396.1.
U89935 Genomic DNA. Translation: AAB64399.1.

PIR

A26772.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BA3	X-ray	2.20	A	1-550	[»]
1LCI	X-ray	2.00	A	1-550	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.13.12.7. 142311.

Family and domain databases

InterPro

IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]

Pfam

PF00501. AMP-binding. 1 hit.
[Graphical view]

PROSITE

PS00455. AMP_BINDING. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

LUCI_PHOPY

Accession

Primary (citable) accession number: P08659
Secondary accession number(s): Q27755

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	November 24, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)