[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0167-4781(93)90172-A; PubMed=8504162 [NCBI, ExPASy, EBI, Israel, Japan] Devine J.H., Kutuzova G.D., Green V.A., Ugarova N.N., Baldwin T.O.; "Luciferase from the east European firefly Luciola mingrelica: cloning and nucleotide sequence of the cDNA, overexpression in Escherichia coli and purification of the enzyme."; Biochim. Biophys. Acta 1173:121-132(1993).
[2]	FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. DOI=10.1002/bio.1170040155; PubMed=2801227 [NCBI, ExPASy, EBI, Israel, Japan] Ugarova N.N.; "Luciferase of Luciola mingrelica fireflies. Kinetics and regulation mechanism."; J. Biolumin. Chemilumin. 4:406-418(1989).
[3]	SUBUNIT. Ugarova N.N., Brovko L. Jr., Belyayeva E.I., Philippova N. Jr., Berezin I.V.; "Dimers as catalytically active particles of firefly luciferase."; Dokl. Akad. Nauk SSSR 260:358-360(1981).

Comments

FUNCTION: Produces green light with a wavelength of 570 nm.
CATALYTIC ACTIVITY: Photinus luciferin + O₂ + ATP = oxidized Photinus luciferin + CO₂ + AMP + diphosphate + light.
COFACTOR: Magnesium.
COFACTOR: Phospholipids.
ENZYME REGULATION: Inhibited by ATP analogs and sodium deoxycholate.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters: K_M=11.5 µM for luciferase;
K_M=130 µM for ATP;
pH dependence: Optimum pH is 7.7;
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Peroxisome (By similarity).
SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

S61961; AAB26932.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S33788; S33788.

3D structure databases

HSSP

P08659; 1LCI. [HSSP ENTRY / PDB]

SMR

Q26304; 6-544.

ModBase

Q26304.

Ontologies

GO:0005777;	Cellular component: peroxisome (inferred from sequence or structural similarity from UniProtKB).
GO:0000287;	Molecular function: magnesium ion binding (inferred from direct assay from UniProtKB).
GO:0047077;	Molecular function: Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) activity (inferred from direct assay from UniProtKB).
GO:0008218;	Biological process: bioluminescence (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.

Pfam

PF00501; AMP-binding; 1.
Pfam graphical view of domain structure.

PRINTS

PR00154; AMPBINDING.

PROSITE

PS00455; AMP_BINDING; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Luminescence; Magnesium; Metal-binding; Monooxygenase; Oxidoreductase; Peroxisome; Photoprotein.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 548`	`548`	`Luciferin 4-monooxygenase.`	`PRO_0000193145`
`MOTIF`	`546 548`	`3`	`Microbody targeting signal (Potential).`

Sequence information

Length: 548 AA [This is the length of the unprocessed precursor]

Molecular weight: 60495 Da [This is the MW of the unprocessed precursor]

CRC64: 62C8953BDFFBC423 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEMEKEENVV YGPLPFYPIE EGSAGIQLHK YMHQYAKLGA IAFSNALTGV DISYQEYFDI 

        70         80         90        100        110        120 
TCRLAEAMKN FGMKPEEHIA LCSENCEEFF IPVLAGLYIG VAVAPTNEIY TLRELNHSLG 

       130        140        150        160        170        180 
IAQPTIVFSS RKGLPKVLEV QKTVTCIKKI VILDSKVNFG GHDCMETFIK KHVELGFQPS 

       190        200        210        220        230        240 
SFVPIDVKNR KQHVALLMNS SGSTGLPKGV RITHEGAVTR FSHAKDPIYG NQVSPGTAIL 

       250        260        270        280        290        300 
TVVPFHHGFG MFTTLGYFAC GYRVVMLTKF DEELFLRTLQ DYKCTSVILV PTLFAILNKS 

       310        320        330        340        350        360 
ELIDKFDLSN LTEIASGGAP LAKEVGEAVA RRFNLPGVRQ GYGLTETTSA FIITPEGDDK 

       370        380        390        400        410        420 
PGASGKVVPL FKVKVIDLDT KKTLGVNRRG EICVKGPSLM LGYSNNPEAT RETIDEEGWL 

       430        440        450        460        470        480 
HTGDIGYYDE DEHFFIVDRL KSLIKYKGYQ VPPAELESVL LQHPNIFDAG VAGVPDPDAG 

       490        500        510        520        530        540 
ELPGAVVVME KGKTMTEKEI VDYVNSQVVN HKRLRGGVRF VDEVPKGLTG KIDAKVIREI 


LKKPQAKM

Q26304 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools