[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=ATCC 33843 / 392 / MAV; PubMed=3514602 [NCBI, ExPASy, EBI, Israel, Japan] Johnston T.C., Thompson R.B., Baldwin T.O.; "Nucleotide sequence of the luxB gene of Vibrio harveyi and the complete amino acid sequence of the beta subunit of bacterial luciferase."; J. Biol. Chem. 261:4805-4811(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12. PubMed=3997817 [NCBI, ExPASy, EBI, Israel, Japan] Cohn D.H., Mileham A.J., Simon M.I., Nealson K.H., Rausch S.K., Bonam D., Baldwin T.O.; "Nucleotide sequence of the luxA gene of Vibrio harveyi and the complete amino acid sequence of the alpha subunit of bacterial luciferase."; J. Biol. Chem. 260:6139-6146(1985).
[3]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). DOI=10.1021/bi00020a002; PubMed=7756289 [NCBI, ExPASy, EBI, Israel, Japan] Fisher A.J., Raushel F.M., Baldwin T.O., Rayment I.; "Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4-A resolution."; Biochemistry 34:6581-6586(1995).
[4]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS). DOI=10.1074/jbc.271.36.21956; PubMed=8703001 [NCBI, ExPASy, EBI, Israel, Japan] Fisher A.J., Thompson T.B., Thoden J.B., Baldwin T.O., Rayment I.; "The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions."; J. Biol. Chem. 271:21956-21968(1996).
[5]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). DOI=10.1021/bi962511x; PubMed=9020763 [NCBI, ExPASy, EBI, Israel, Japan] Tanner J.J., Miller M.D., Wilson K.S., Tu S.C., Krause K.L.; "Structure of bacterial luciferase beta 2 homodimer: implications for flavin binding."; Biochemistry 36:665-672(1997).
[6]	X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS). PubMed=9007973 [NCBI, ExPASy, EBI, Israel, Japan] Thoden J.B., Holden H.M., Fisher A.J., Sinclair J.F., Wesenberg G., Baldwin T.O., Rayment I.; "Structure of the beta 2 homodimer of bacterial luciferase from Vibrio harveyi: X-ray analysis of a kinetic protein folding trap."; Protein Sci. 6:13-23(1997).

Comments

FUNCTION: Light-emitting reaction in luminous bacteria. The specific role of the beta subunit is unknown, but it is absolutely required for bioluminescence activity.
CATALYTIC ACTIVITY: RCHO + reduced FMN + O₂ = RCOOH + FMN + H₂O + light.
SUBUNIT: Heterodimer of an alpha and a beta chain.
SIMILARITY: Belongs to the bacterial luciferase oxidoreductase 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

M10961; AAA88686.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A23866; A23866.

3D structure databases

PDB

1BRL; X-ray; 2.40 A; B/D=1-324.	[ExPASy / RCSB / EBI]
1BSL; X-ray; 1.95 A; A/B=1-324.	[ExPASy / RCSB / EBI]
1LUC; X-ray; 1.50 A; B=1-324.	[ExPASy / RCSB / EBI]
1XKJ; X-ray; 2.50 A; A/B=1-324.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BRL; -.
1BSL; -.
1LUC; -.
1XKJ; -.

ModBase

P07739.

Family and domain databases

InterPro

IPR011251; Luciferase-like_bac.
IPR002103; Luciferase_bac.
IPR016048; Luciferase_mOase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.30; Luciferase_like; 1.

Pfam

PF00296; Bac_luciferase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00089; LUCIFERASE.

PROSITE

PS00494; BACTERIAL_LUCIFERASE; 1.

Other

P07739; -.

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

Keywords

3D-structure; Direct protein sequencing; Flavoprotein; FMN; Luminescence; Monooxygenase; Oxidoreductase; Photoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 324`	`324`	`Alkanal monooxygenase beta chain.`	`PRO_0000220181`
`STRAND`	`2 7`	`6`
`STRAND`	`13 15`	`3`
`HELIX`	`17 32`	`16`
`TURN`	`33 35`	`3`
`STRAND`	`38 41`	`4`
`STRAND`	`46 49`	`4`
`HELIX`	`55 65`	`11`
`STRAND`	`70 77`	`8`
`HELIX`	`83 97`	`15`
`STRAND`	`101 106`	`6`
`HELIX`	`111 116`	`6`
`HELIX`	`124 141`	`18`
`STRAND`	`142 144`	`3`
`STRAND`	`148 150`	`3`
`STRAND`	`168 174`	`7`
`HELIX`	`177 185`	`9`
`STRAND`	`190 192`	`3`
`HELIX`	`198 215`	`18`
`STRAND`	`225 232`	`8`
`HELIX`	`236 254`	`19`
`HELIX`	`260 270`	`11`
`STRAND`	`271 275`	`5`
`HELIX`	`276 290`	`15`
`STRAND`	`293 298`	`6`
`HELIX`	`305 318`	`14`

Sequence information

Length: 324 AA [This is the length of the unprocessed precursor]

Molecular weight: 36345 Da [This is the MW of the unprocessed precursor]

CRC64: 974FF37653C052D3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFGLFFLNF MNSKRSSDQV IEEMLDTAHY VDQLKFDTLA VYENHFSNNG VVGAPLTVAG 

        70         80         90        100        110        120 
FLLGMTKNAK VASLNHVITT HHPVRVAEEA CLLDQMSEGR FAFGFSDCEK SADMRFFNRP 

       130        140        150        160        170        180 
TDSQFQLFSE CHKIINDAFT TGYCHPNNDF YSFPKISVNP HAFTEGGPAQ FVNATSKEVV 

       190        200        210        220        230        240 
EWAAKLGLPL VFRWDDSNAQ RKEYAGLYHE VAQAHGVDVS QVRHKLTLLV NQNVDGEAAR 

       250        260        270        280        290        300 
AEARVYLEEF VRESYSNTDF EQKMGELLSE NAIGTYEEST QAARVAIECC GAADLLMSFE 

       310        320 
SMEDKAQQRA VIDVVNANIV KYHS

P07739 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