Reviewed,
UniProtKB/Swiss-Prot P29334 (LUXE_PHOLE)
Last modified
June 16, 2009.
Version 40.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Long-chain-fatty-acid--luciferin-component ligase EC=6.2.1.19 Alternative name(s): Acyl-protein synthetase | ||
| Gene names |
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| Organism | Photobacterium leiognathi | ||
| Taxonomic identifier | 658 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Photobacterium |
Protein attributes
| Sequence length | 373 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Acyl-protein synthetase activates tetradecanoic acid. It is a component of the fatty acid reductase complex responsible for converting tetradecanoic acid to the aldehyde which serves as substrate in the luciferase-catalyzed reaction. |
| Catalytic activity | ATP + an acid + protein = AMP + diphosphate + an acyl-protein thioester. |
| Pathway | |
| Sequence similarities | Belongs to the luxE family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Luminescence |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Gene Ontology (GO) | |
| Biological process | bioluminescence Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-luciferin-component ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 373 | 373 | Long-chain-fatty-acid--luciferin-component ligase | PRO_0000208063 | |||
Sequences
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References
| [1] | "The lux genes of the luminous bacterial symbiont, Photobacterium leiognathi, of the ponyfish. Nucleotide sequence, difference in gene organization, and high expression in mutant Escherichia coli." Lee C.Y., Szittner R.B., Meighen E.A. Eur. J. Biochem. 201:161-167(1991) [PubMed: 1915359] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 25521 / L1 / CIP 665. |
Cross-references
Sequence databases | |
|---|---|
| M63594 Genomic DNA. Translation: AAA25620.1. | |
| PIR | S17955. |
3D structure databases | |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 6.2.1.19. 349. |
Family and domain databases | |
| InterPro | IPR016671. Acyl-protein_synth_LuxE_bac. IPR007534. LuxE. [Graphical view] |
| Pfam | PF04443. LuxE. 1 hit. [Graphical view] |
| PIRSF | PIRSF016580. Acyl-protein_synthetase_LuxE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LUXE_PHOLE | ||||||||
| Accession | Primary (citable) accession number: P29334 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (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 |

Clusters with


