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Reviewed, UniProtKB/Swiss-Prot Q26304 (LUCI_LUCMI)

Last modified June 16, 2009. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Luciferin 4-monooxygenase
      Short name=Luciferase
    EC=1.13.12.7
OrganismLuciola mingrelica (Southern Russian firefly)
Taxonomic identifier27446 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaColeopteraPolyphagaElateriformiaElateroideaLampyridaeLuciolinaeLuciola

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Produces green light with a wavelength of 570 nm. Ref.2

Catalytic activity

Photinus luciferin + O2 + ATP = oxidized Photinus luciferin + CO2 + AMP + diphosphate + light. Ref.2

Cofactor

Magnesium. Ref.2

Phospholipids. Ref.2

Enzyme regulation

Inhibited by ATP analogs and sodium deoxycholate. Ref.2

Subunit structure

Homodimer. Ref.3

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

biophysicochemical properties

Kinetic parameters:

KM=11.5 µM for luciferase Ref.2

KM=130 µM for ATP Ref.2

pH dependence:

Optimum pH is 7.7. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 548548Luciferin 4-monooxygenase
PRO_0000193145

Regions

Motif546 – 5483Microbody targeting signal Potential

Sequences

Sequence LengthMass (Da)Tools
Q26304-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 62C8953BDFFBC423

FASTA54860,495
        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 

« Hide

References

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

Cross-references

Sequence databases

S61961 mRNA. Translation: AAB26932.1.
PIRS33788.

3D structure databases

HSSPHSSP built from PDB template 1LCI based on UniProtKB P08659.
SMRQ26304. Positions 6-544.
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.13.12.7. 229293.

Family and domain databases

InterProIPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLUCI_LUCMI
AccessionPrimary (citable) accession number: Q26304
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents