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Reviewed, UniProtKB/Swiss-Prot P19841 (LUXC_PHOPO)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    Acyl-CoA reductase
    EC=1.2.1.50
Gene names
Name: luxC
OrganismPhotobacterium phosphoreum
Taxonomic identifier659 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaePhotobacterium

Protein attributes

Sequence length382 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

LuxC is the fatty acid reductase enzyme responsible for synthesis of the aldehyde substrate for the luminescent reaction catalyzed by luciferase.

Catalytic activity

A long-chain aldehyde + CoA + NADP+ = a long-chain acyl-CoA + NADPH.

Pathway

Lipid metabolism; bioluminescent fatty acid reduction.

Sequence similarities

Belongs to the luxC family.

Ontologies

Keywords
   Biological processLuminescence
   LigandNADP
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processbioluminescence

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionacyl-CoA reductase activity

Inferred from electronic annotation. Source: InterPro

long-chain-fatty-acyl-CoA reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 382382Acyl-CoA reductase
PRO_0000220200

Experimental info

Non-adjacent residues371 – 3722

Sequences

Sequence LengthMass (Da)Tools
P19841-1 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: B6C6316B49030EE9

FASTA38243,085
        10         20         30         40         50         60 
MCNAEFKGDC MIKKIPMIIG GAERDTSEHE YRELTLNSYK VSIPIINQDD VEAIKSQNVE 

        70         80         90        100        110        120 
NNLNINQIVN FLYTVGQKWK SENYSRRLTY IRDLVRFLGY SPEMAKLEAN WISMILSSKS 

       130        140        150        160        170        180 
ALYDIVETEL GSRHIVDEWL PQGDCYVKAM PKGKSVHLLA GNVPLSGVTS IIRAILTKNE 

       190        200        210        220        230        240 
CIIKTSSADP FTAIALASSF IDTDEHHPIS RSMSVMYWSH NEDIAIPQQI MNCADVVVSW 

       250        260        270        280        290        300 
GGYDAIKWAT EHTPVNVDIL KFGPKKSIAI VDNPVDITAS AIGVAHDICF YDQQACFSTQ 

       310        320        330        340        350        360 
DIYYIGDNID AFFDELVEQL NLYMDILPKG DQTFDEKASF SLIEKECQFA KYKVEKGDNQ 

       370        380 
SWLLVKSPLG SLEEDKFLVF VP 

« Hide

References

[1]"The lumazine protein gene in Photobacterium phosphoreum is linked to the lux operon."
Prasher D.C., O'Kane D., Lee J., Woodward B.
Nucleic Acids Res. 18:6450-6450(1990) [PubMed: 2243804] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-371.
Strain: A13.
[2]"A lux-specific myristoyl transferase in luminescent bacteria related to eukaryotic serine esterases."
Ferri S.R., Meighen E.A.
J. Biol. Chem. 266:12852-12857(1991) [PubMed: 2071574] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 372-382.

Cross-references

Sequence databases

X54690 Genomic DNA. Translation: CAA38506.1.
M64224 Genomic DNA. Translation: AAA25625.1.
PIRB39853.
S12116.

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA1.2.1.50. 348.

Family and domain databases

InterProIPR016162. Ald_DH_N.
IPR008670. LuxC.
[Graphical view]
Gene3DG3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PfamPF05893. LuxC. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLUXC_PHOPO
AccessionPrimary (citable) accession number: P19841
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1995
Last modified: June 16, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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