[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0006-291X(91)90959-B; PubMed=2018544 [NCBI, ExPASy, EBI, Israel, Japan] Ferri S.R., Soly R.R., Szittner R.B., Meighen E.A.; "Structure and properties of luciferase from Photobacterium phosphoreum."; Biochem. Biophys. Res. Commun. 176:541-548(1991).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41. PubMed=2071574 [NCBI, ExPASy, EBI, Israel, Japan] Ferri S.R., Meighen E.A.; "A lux-specific myristoyl transferase in luminescent bacteria related to eukaryotic serine esterases."; J. Biol. Chem. 266:12852-12857(1991).

Comments

FUNCTION: Light-emitting reaction in luminous bacteria.
CATALYTIC ACTIVITY: RCHO + reduced FMN + O₂ = RCOOH + FMN + H₂O + light.
SUBUNIT: Heterodimer of an alpha and a beta chain.

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

M65067; AAA70297.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M64224; AAA25627.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JH0387; JH0387.

3D structure databases

HSSP

P07740; 1LUC. [HSSP ENTRY / PDB]

ModBase

P24113.

Ontologies

GO:0047646;	Molecular function: alkanal monooxygenase (FMN-linked) activity (inferred from electronic annotation from EC).
GO:0008218;	Biological process: bioluminescence (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.

ProtoNet

P24113.

Genome annotation databases

KEGG

son:SO_1467; -.

Other

UniRef

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

Keywords

Flavoprotein; FMN; Luminescence; Monooxygenase; Oxidoreductase; Photoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 346`	`346`	`Alkanal monooxygenase alpha chain.`	`PRO_0000220169`
`CONFLICT`	`6 6`		`I -> IC (in Ref. 2; AAA25627).`
`CONFLICT`	`40 41`		`LE -> TL (in Ref. 2; AAA25627).`

Sequence information

Length: 346 AA [This is the length of the unprocessed precursor]

Molecular weight: 39364 Da [This is the MW of the unprocessed precursor]

CRC64: 360EC324E0A438A0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKFGNIFSYQ PPGESHKEVM DRFVRLGVAS EELNFDTYWL EHHFTEFGLT GNLFVACANL 

        70         80         90        100        110        120 
LGRTTKLNVG TMIVLPTAHP ARQMEDLLLL DQMSKGRFNF GVVRGYHKDF RVFGVTMEDS 

       130        140        150        160        170        180 
RAITEDFHTM IMDGTKTGLH TDGKNIEFPD VNVYPEAYLE KIPTCMTAES ATTTWLAERG 

       190        200        210        220        230        240 
LPMVLSWIIT TSEKKAQMEL YNAVRDSGYS EEYIKNVDHS MTLICSVDED GKKAEDVREF 

       250        260        270        280        290        300 
LGNWYDSYVN ATNIFSESNQ TRGYDYHKGQ KDFVLQGHTN TKRRVDYSND LNPVGTPEKC 

       310        320        330        340 
IEIQRDIDAT GITNITLGFE ANGSEEEIIA SMKRFMQVAP FLKDPK

P24113 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