EzCatDB: D00489
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DB codeD00489
CATH domainDomain 13.20.20.30 : TIM BarrelCatalytic domain
Domain 23.20.20.30 : TIM Barrel
E.C.1.14.14.3
CSA1luc
MACiEM0132


Enzyme Name
UniProtKBKEGG

P07739P07740
Protein nameAlkanal monooxygenase beta chainAlkanal monooxygenase alpha chainalkanal monooxygenase (FMN-linked)
bacterial luciferase
aldehyde monooxygenase
luciferase
Vibrio fischeri luciferase
SynonymsEC 1.14.14.3
Bacterial luciferase beta chain
EC 1.14.14.3
Bacterial luciferase alpha chain
PfamPF00296 (Bac_luciferase)
[Graphical view]
PF00296 (Bac_luciferase)
[Graphical view]


UniProtKB:Accession NumberP07739P07740
Entry nameLUXB_VIBHALUXA_VIBHA
ActivityRCHO + reduced FMN + O(2) = RCOOH + FMN + H(2)O + light.RCHO + reduced FMN + O(2) = RCOOH + FMN + H(2)O + light.
SubunitHeterodimer of an alpha and a beta chain.Heterodimer of an alpha and a beta chain.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00071C01847C00007C00060C00061C00001C00205
CompoundMagnesiumAldehydeReduced FMNO2CarboxylateFMNH2Ohn(light)
Typedivalent metal (Ca2+, Mg2+)carbohydrateamide group,amine group,aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionotherscarboxyl groupamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ionH2Oothers
ChEBI18420

16048
15379
26689
27140

17621
15377

PubChem888

101960650
445395
711
977

643976
22247451
962

                
1brlAUnboundUnboundUnboundUnboundUnboundUnbound  
1lucABound:_MGUnboundUnboundUnboundUnboundUnbound  
1brlBUnboundUnboundUnboundUnboundUnboundUnbound  
1bslAUnboundUnboundUnboundUnboundUnboundUnbound  
1bslBUnboundUnboundUnboundUnboundUnboundUnbound  
1lucBBound:_MGUnboundUnboundUnboundUnboundUnbound  
1xkjAUnboundUnboundUnboundUnboundUnboundUnbound  
1xkjBUnboundUnboundUnboundUnboundUnboundUnbound  

Active-site residues
resource
literature [17], [20], [21], [26] & [33]
pdbCatalytic residuesCofactor-binding residuesMain-chain involved in catalysis
           
1brlAHIS 44;HIS 45;CYS 106;ASP 113;PHE 261
GLU  19(Magnesium binding)
ALA 74;ALA 75
1lucAHIS 44;HIS 45;CYS 106;ASP 113;PHE 261
GLU  19(Magnesium binding)
ALA 74;ALA 75
1brlB 
GLU 237(Magnesium binding)
 
1bslA 
GLU 237(Magnesium binding)
 
1bslB 
GLU 237(Magnesium binding)
 
1lucB 
GLU 237(Magnesium binding)
 
1xkjA 
GLU 237(Magnesium binding)
 
1xkjB 
GLU 237(Magnesium binding)
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]SCHEME I
[7]SCHEME I, SCHEME II
[9]Scheme 1
[11]p.1771-1773
[12]Scheme 1, p.12199-12200
[13]p.1920
[14]p.6584-6586
[16]Fig.1
[17]p.1967
[18]SCHEME I, SCHEME II, SCHEME III, SCHEME IV, SCHEME VI, p.108-110
[20]Scheme 1, p.14612-14614
[21]p.671-672
[23]Fig.1, Fig.9, p.2604-2605
[26]Scheme I, p.4413-4415
[31]p.1566-1569
[33]Scheme 1, p.1728-2730

references
[1]
PubMed ID5161031
JournalBiochemistry
Year1971
Volume10
Pages4069-73
AuthorsMeighen EA, Nicoli MZ, Hastings JW
TitleFunctional differences of the nonidentical subunits of bacterial luciferase. Properties of hybrids of native and chemically modified bacterial luciferase.
[2]
PubMed ID5056080
JournalBiochemistry
Year1972
Volume11
Pages3359-70
AuthorsCline TW, Hastings JW
TitleMutationally altered bacterial luciferase. Implications for subunit functions.
[3]
PubMed ID4822498
JournalJ Biol Chem
Year1974
Volume249
Pages2385-92
AuthorsNicoli MZ, Meighen EA, Hastings JW
TitleBacterial luciferase. Chemistry of the reactive sulfhydryl.
[4]
PubMed ID6965792
JournalProc Natl Acad Sci U S A
Year1980
Volume77
Pages249-52
AuthorsTu SC, Hastings JW
TitlePhysical interaction and activity coupling between two enzymes induced by immobilization of one.
[5]
PubMed ID3968061
JournalJ Biol Chem
Year1985
Volume260
Pages1287-9
AuthorsSwanson R, Weaver LH, Remington SJ, Matthews BW, Baldwin TO
TitleCrystals of luciferase from Vibrio harveyi. A preliminary characterization.
[6]
PubMed ID2307667
JournalJ Biol Chem
Year1990
Volume265
Pages4200-3
AuthorsXi L, Cho KW, Herndon ME, Tu SC
TitleElicitation of an oxidase activity in bacterial luciferase by site-directed mutation of a noncatalytic residue.
[7]
PubMed ID1567836
JournalBiochemistry
Year1992
Volume31
Pages3807-13
AuthorsAbu-Soud H, Mullins LS, Baldwin TO, Raushel FM
TitleStopped-flow kinetic analysis of the bacterial luciferase reaction.
[8]
PubMed ID1560468
JournalJ Mol Biol
Year1992
Volume224
Pages523-6
AuthorsMoore SA, James MN, O'Kane DJ, Lee J
TitleCrystallization of Photobacterium leiognathi non-fluorescent flavoprotein, an unusual flavoprotein with limited sequence identity to bacterial luciferase.
[9]
PubMed ID8422349
JournalBiochemistry
Year1993
Volume32
Pages404-11
AuthorsEckstein JW, Hastings JW, Ghisla S
TitleMechanism of bacterial bioluminescence: 4a,5-dihydroflavin analogs as models for luciferase hydroperoxide intermediates and the effect of substituents at the 8-position of flavin on luciferase kinetics.
[10]
PubMed ID8494880
JournalBiochemistry
Year1993
Volume32
Pages5036-44
AuthorsSinclair JF, Waddle JJ, Waddill EF, Baldwin TO
TitlePurified native subunits of bacterial luciferase are active in the bioluminescence reaction but fail to assemble into the alpha beta structure.
[11]
PubMed ID8491169
JournalEMBO J
Year1993
Volume12
Pages1767-74
AuthorsMoore SA, James MN, O'Kane DJ, Lee J
TitleCrystal structure of a flavoprotein related to the subunits of bacterial luciferase.
[12]
PubMed ID7918440
JournalBiochemistry
Year1994
Volume33
Pages12194-201
AuthorsXin X, Xi L, Tu SC
TitleProbing the Vibrio harveyi luciferase beta subunit functionality and the intersubunit domain by site-directed mutagenesis.
[13]
PubMed ID7703838
JournalProtein Sci
Year1994
Volume3
Pages1914-26
AuthorsMoore SA, James MN
TitleCommon structural features of the luxF protein and the subunits of bacterial luciferase: evidence for a (beta alpha)8 fold in luciferase.
[14]
CommentsX-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)
Medline ID95275854
PubMed ID7756289
JournalBiochemistry
Year1995
Volume34
Pages6581-6
AuthorsFisher AJ, Raushel FM, Baldwin TO, Rayment I
TitleThree-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 A resolution.
Related PDB1brl
Related UniProtKBP07739,P07740
[15]
PubMed ID7578121
JournalBiochemistry
Year1995
Volume34
Pages15084-90
AuthorsLi Z, Meighen EA
TitleTryptophan 250 on the alpha subunit plays an important role in flavin and aldehyde binding to bacterial luciferase. Effects of W-->Y mutations on catalytic function.
[16]
PubMed ID8749369
JournalCurr Opin Struct Biol
Year1995
Volume5
Pages798-809
AuthorsBaldwin TO, Christopher JA, Raushel FM, Sinclair JF, Ziegler MM, Fisher AJ, Rayment I
TitleStructure of bacterial luciferase.
[17]
CommentsX-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS)
Medline ID96355591
PubMed ID8703001
JournalJ Biol Chem
Year1996
Volume271
Pages21956-68
AuthorsFisher AJ, Thompson TB, Thoden JB, Baldwin TO, Rayment I
TitleThe 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions.
Related PDB1luc
Related UniProtKBP07739,P07740
[18]
PubMed ID8550543
JournalJ Biol Chem
Year1996
Volume271
Pages104-10
AuthorsFrancisco WA, Abu-Soud HM, Topgi R, Baldwin TO, Raushel FM
TitleInteraction of bacterial luciferase with 8-substituted flavin mononucleotide derivatives.
[19]
PubMed ID9048575
JournalBiochemistry
Year1997
Volume36
Pages1891-9
AuthorsClark AC, Raso SW, Sinclair JF, Ziegler MM, Chaffotte AF, Baldwin TO
TitleKinetic mechanism of luciferase subunit folding and assembly.
[20]
PubMed ID9402752
JournalBiochemistry
Year1997
Volume36
Pages14609-15
AuthorsHuang S, Tu SC
TitleIdentification and characterization of a catalytic base in bacterial luciferase by chemical rescue of a dark mutant.
[21]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID97172895
PubMed ID9020763
JournalBiochemistry
Year1997
Volume36
Pages665-72
AuthorsTanner JJ, Miller MD, Wilson KS, Tu SC, Krause KL
TitleStructure of bacterial luciferase beta 2 homodimer: implications for flavin binding.
Related PDB1xkj
Related UniProtKBP07739
[22]
CommentsX-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS)
Medline ID97160473
PubMed ID9007973
JournalProtein Sci
Year1997
Volume6
Pages13-23
AuthorsThoden JB, Holden HM, Fisher AJ, Sinclair JF, Wesenberg G, Baldwin TO, Rayment I
TitleStructure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap.
Related PDB1bsl
Related UniProtKBP07739,P07740
[23]
PubMed ID9485410
JournalBiochemistry
Year1998
Volume37
Pages2596-606
AuthorsFrancisco WA, Abu-Soud HM, DelMonte AJ, Singleton DA, Baldwin TO, Raushel FM
TitleDeuterium kinetic isotope effects and the mechanism of the bacterial luciferase reaction.
[24]
PubMed ID9622513
JournalBiochemistry
Year1998
Volume37
Pages8614
AuthorsHuang S, Tu SC
TitleIdentification and characterization of a catalytic base in bacterial luciferase by chemical rescue of a dark mutant
[25]
PubMed ID10328774
JournalAnal Biochem
Year1999
Volume270
Pages133-9
AuthorsMin DJ, Andrade JD, Stewart RJ
TitleSpecific immobilization of in vivo biotinylated bacterial luciferase and FMN:NAD(P)H oxidoreductase.
[26]
PubMed ID10194361
JournalBiochemistry
Year1999
Volume38
Pages4409-15
AuthorsLi H, Ortego BC, Maillard KI, Willson RC, Tu SC
TitleEffects of mutations of the alpha His45 residue of Vibrio harveyi luciferase on the yield and reactivity of the flavin peroxide intermediate.
[27]
PubMed ID10587436
JournalBiochemistry
Year1999
Volume38
Pages16136-45
AuthorsNoland BW, Dangott LJ, Baldwin TO
TitleFolding, stability, and physical properties of the alpha subunit of bacterial luciferase.
[28]
PubMed ID10721898
JournalJ Nutr
Year2000
Volume130
Pages331S-332S
AuthorsTu SC, Lei B, Liu M, Tang CK, Jeffers C
TitleProbing the mechanisms of the biological intermolecular transfer of reduced flavin.
[29]
PubMed ID11735398
JournalBiochemistry
Year2001
Volume40
Pages15153-63
AuthorsApuy JL, Park ZY, Swartz PD, Dangott LJ, Russell DH, Baldwin TO
TitlePulsed-alkylation mass spectrometry for the study of protein folding and dynamics: development and application to the study of a folding/unfolding intermediate of bacterial luciferase.
[30]
PubMed ID11735428
JournalBiochemistry
Year2001
Volume40
Pages15436-43
AuthorsSparks JM, Baldwin TO
TitleFunctional implications of the unstructured loop in the (beta/alpha)(8) barrel structure of the bacterial luciferase alpha subunit.
[31]
PubMed ID11468353
JournalProtein Sci
Year2001
Volume10
Pages1563-71
AuthorsLin LY, Sulea T, Szittner R, Vassilyev V, Purisima EO, Meighen EA
TitleModeling of the bacterial luciferase-flavin mononucleotide complex combining flexible docking with structure-activity data.
[32]
PubMed ID11900533
JournalBiochemistry
Year2002
Volume41
Pages3906-15
AuthorsInlow JK, Baldwin TO
TitleMutational analysis of the subunit interface of Vibrio harveyi bacterial luciferase.
[33]
PubMed ID11827516
JournalBiochemistry
Year2002
Volume41
Pages1724-31
AuthorsLow JC, Tu SC
TitleFunctional roles of conserved residues in the unstructured loop of Vibrio harveyi bacterial luciferase.
[34]
PubMed ID12445781
JournalJ Mol Biol
Year2002
Volume324
Pages457-68
AuthorsEichhorn E, Davey CA, Sargent DF, Leisinger T, Richmond TJ
TitleCrystal structure of Escherichia coli alkanesulfonate monooxygenase SsuD.
[35]
PubMed ID12627978
JournalBiochemistry
Year2003
Volume42
Pages3105-12
AuthorsNoland BW, Baldwin TO
TitleDemonstration of two independently folding domains in the alpha subunit of bacterial luciferase by preferential ligand binding-induced stabilization.

comments
This enzyme is composed of two distinct but homologous chains.
Although this enzyme can bind two magnesium ions, they are distant from the active site and not involved in catalysis.
The peptide bond between Ala74-Ala75, which is located at the active-site, has a cis conformation, which is extremely rare for non-proryl peptide bond (see [17]).
E.C. 1.13.12.7 is Another luciferase (firefly luciferase, M00009).

createdupdated
2004-02-192009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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