DB code: M00009

CATH domain 3.40.50.980 : Rossmann fold
3.40.50.980 : Rossmann fold Catalytic domain
2.30.38.10 : Luciferase; domain 3
3.30.300.30 : GMP Synthetase; Chain A, domain 3 Catalytic domain
4.10.8.10 : Luciferase; domain 5
E.C. 1.13.12.7
CSA 1lci
M-CSA 1lci
MACiE M0128

CATH domain Related DB codes (homologues)
2.30.38.10 : Luciferase; domain 3 M00170 M00347
3.30.300.30 : GMP Synthetase; Chain A, domain 3 M00170 M00347
3.40.50.980 : Rossmann fold M00170 M00347

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P08659 Luciferin 4-monooxygenase
Luciferase
EC 1.13.12.7
PF00501 (AMP-binding)
[Graphical View]

KEGG enzyme name
Photinus-luciferin 4-monooxygenase (ATP-hydrolysing)
firefly luciferase
luciferase (firefly luciferin)
Photinus luciferin 4-monooxygenase (adenosinetriphosphate-hydrolyzing)
firefly luciferin luciferase
Photinus pyralis luciferase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P08659 LUCI_PHOPY Photinus luciferin + O(2) + ATP = oxidized Photinus luciferin + CO(2) + AMP + diphosphate + light. Peroxisome. Magnesium.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C02740 C00007 C00002 C03797 C00011 C00020 C00013 C00205
E.C.
Compound Magnesium Photinus luciferin O2 ATP Oxidized Photinus luciferin CO2 AMP Pyrophosphate hn(light)
Type divalent metal (Ca2+, Mg2+) amine group,aromatic ring (only carbon atom),carboxyl group,aromatic ring (with hetero atoms other than nitrogen atoms),sulfide group others amine group,nucleotide amine group,aromatic ring (only carbon atom),aromatic ring (with hetero atoms other than nitrogen atoms),sulfide group others amine group,nucleotide phosphate group/phosphate ion others
ChEBI 18420
17165
27140
26689
15379
15422
16792
16526
16027
29888
PubChem 888
977
5957
280
6083
21961011
1023
1ba3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lciA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ba3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lciA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ba3A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lciA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ba3A04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lciA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ba3A05 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1lciA05 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [4], [7], [11], [14]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ba3A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lciA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ba3A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 218;HIS 245;THR 343
1lciA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 218;HIS 245;THR 343
1ba3A03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lciA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1ba3A04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 529
1lciA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain LYS 529
1ba3A05 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1lciA05 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[2]
Fig.3, p.224-225
[3]
p.292-295
[4]
Fig.1, Fig.5, p.15316-15318
[7]
Fig.1, Fig.5, p.132270-13228
[11]
Fig.1, Fig.2, p.5439
[14]
Fig.1, p.2416-2417
[16]
Fig.3, Fig.7, p.1837-1838
[18]
Fig.1, p.10434

References
[1]
Resource
Comments
Medline ID
PubMed ID 8547353
Journal Biochim Biophys Acta
Year 1996
Volume 1292
Pages 89-98
Authors Waud JP, Sala-Newby GB, Matthews SB, Campbell AK
Title Engineering the C-terminus of firefly luciferase as an indicator of covalent modification of proteins.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8805542
Journal Structure
Year 1996
Volume 4
Pages 223-8
Authors Baldwin TO
Title Firefly luciferase: the structure is known, but the mystery remains.
Related PDB
Related UniProtKB
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 96398615
PubMed ID 8805533
Journal Structure
Year 1996
Volume 4
Pages 287-98
Authors Conti E, Franks NP, Brick P
Title Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes.
Related PDB 1lci
Related UniProtKB P08659
[4]
Resource
Comments
Medline ID
PubMed ID 9799491
Journal Biochemistry
Year 1998
Volume 37
Pages 15311-9
Authors Branchini BR, Magyar RA, Murtiashaw MH, Anderson SM, Zimmer M
Title Site-directed mutagenesis of histidine 245 in firefly luciferase: a proposed model of the active site.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS)
Medline ID 99007339
PubMed ID 9788915
Journal Biophys J
Year 1998
Volume 75
Pages 2205-11
Authors Franks NP, Jenkins A, Conti E, Lieb WR, Brick P
Title Structural basis for the inhibition of firefly luciferase by a general anesthetic.
Related PDB 1ba3
Related UniProtKB P08659
[6]
Resource
Comments
Medline ID
PubMed ID 9825705
Journal Photochem Photobiol
Year 1998
Volume 68
Pages 749-53
Authors Sung D, Kang H
Title The N-terminal amino acid sequences of the firefly luciferase are important for the stability of the enzyme.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10529195
Journal Biochemistry
Year 1999
Volume 38
Pages 13223-30
Authors Branchini BR, Magyar RA, Murtiashaw MH, Anderson SM, Helgerson LC, Zimmer M
Title Site-directed mutagenesis of firefly luciferase active site amino acids: a proposed model for bioluminescence color.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10498816
Journal Biochemistry (Mosc)
Year 1999
Volume 64
Pages 962-7
Authors Sandalova TP, Ugarova NN
Title Model of the active site of firefly luciferase.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10404229
Journal Nat Struct Biol
Year 1999
Volume 6
Pages 697-705
Authors Frydman J, Erdjument-Bromage H, Tempst P, Hartl FU
Title Co-translational domain folding as the structural basis for the rapid de novo folding of firefly luciferase.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 10623630
Journal Biochem Biophys Res Commun
Year 2000
Volume 267
Pages 394-7
Authors Kumita JR, Jain L, Safroneeva E, Woolley GA
Title A cysteine-free firefly luciferase retains luminescence activity.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 10820015
Journal Biochemistry
Year 2000
Volume 39
Pages 5433-40
Authors Branchini BR, Murtiashaw MH, Magyar RA, Anderson SM
Title The role of lysine 529, a conserved residue of the acyl-adenylate-forming enzyme superfamily, in firefly luciferase.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11225787
Journal Fresenius J Anal Chem
Year 2000
Volume 366
Pages 760-8
Authors Lewis JC, Daunert S
Title Photoproteins as luminescent labels in binding assays.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11263966
Journal Biochem Biophys Res Commun
Year 2001
Volume 282
Pages 28-33
Authors Wang WQ, Xu Q, Shan YF, Xu GJ
Title Probing local conformational changes during equilibrium unfolding of firefly luciferase: fluorescence and circular dichroism studies of single tryptophan mutants.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11327861
Journal Biochemistry
Year 2001
Volume 40
Pages 2410-8
Authors Branchini BR, Magyar RA, Murtiashaw MH, Portier NC
Title The role of active site residue arginine 218 in firefly luciferase bioluminescence.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11180660
Journal Luminescence
Year 2001
Volume 16
Pages 57-63
Authors Eu J, Andrade J
Title Properties of firefly luciferase immobilized through a biotin carboxyl carrier protein domain.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 12530517
Journal Cell Mol Life Sci
Year 2002
Volume 59
Pages 1833-50
Authors Viviani VR
Title The origin, diversity, and structure function relationships of insect luciferases.
Related PDB
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 12007636
Journal Int J Biochem Cell Biol
Year 2002
Volume 34
Pages 983-91
Authors Wang XC, Yang J, Huang W, He L, Yu JT, Lin QS, Li W, Zhou HM
Title Effects of removal of the N-terminal amino acid residues on the activity and conformation of firefly luciferase.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 12950169
Journal Biochemistry
Year 2003
Volume 42
Pages 10429-36
Authors Branchini BR, Southworth TL, Murtiashaw MH, Boije H, Fleet SE
Title A mutagenesis study of the putative luciferin binding site residues of firefly luciferase.
Related PDB
Related UniProtKB

Comments
This enzyme catalyzes three reactions (see [2]):
(1) Transfer of AMP to the carboxyl group of luciferin compound.
(2) Oxygenation of the compound, resulting in the release of AMP.
(3) Elimination of CO2, leading to formation of an additional double-bond.

Created Updated
2004-10-25 2009-02-26