Reviewed,
UniProtKB/Swiss-Prot Q9PN97 (LUXS_CAMJE)
Last modified
January 19, 2010.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: S-ribosylhomocysteine lyase EC=4.4.1.21 Alternative name(s): Autoinducer-2 production protein luxS AI-2 synthesis protein | ||||
| Gene names |
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| Organism | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 197 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 164 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). Ref.2 |
| Catalytic activity | S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. HAMAP MF_00091 |
| Cofactor | Binds 1 iron ion per subunit By similarity. HAMAP MF_00091 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00091 |
| Sequence similarities | Belongs to the luxS family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Autoinducer synthesis Quorum sensing |
| Ligand | Iron Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | quorum sensing Inferred from electronic annotation. Source: HAMAP |
| Molecular function | S-ribosylhomocysteine lyase activity Inferred from electronic annotation. Source: HAMAP iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 164 | 164 | S-ribosylhomocysteine lyase HAMAP MF_00091 | PRO_0000172214 | |||||
Sites | |||||||||
| Metal binding | 54 | 1 | Iron By similarity | ||||||
| Metal binding | 58 | 1 | Iron By similarity | ||||||
| Metal binding | 128 | 1 | Iron By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
| [2] | "Quorum sensing in Campylobacter jejuni: detection of a luxS encoded signalling molecule." Elvers K.T., Park S.F. Microbiology 148:1475-1481(2002) [PubMed: 11988522] [Abstract] Cited for: FUNCTION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL111168 Genomic DNA. Translation: CAL35313.1. |
| PIR | H81325. |
| RefSeq | YP_002344589.1. |
3D structure databases | |
| SMR | Q9PN97. Positions 3-163. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9PN97. 32 interactions. |
Genome annotation databases | |
| GeneID | 905488. |
| GenomeReviews | Gene locus Cj1198 in contig AL111168_GR. |
| KEGG | cje:Cj1198. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG347473. |
| OMA | VRIAKTM. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ1198-MONOMER. |
| BRENDA | 4.4.1.21. 255835. |
Family and domain databases | |
| HAMAP | MF_00091. LuxS. [Tree] |
| InterPro | IPR011249. Metalloenz_metal-bd. IPR003815. S-ribosylhomocysteinase. [Graphical view] |
| Gene3D | G3DSA:3.30.1360.80. S-ribosylhomocysteinase. 1 hit. |
| Pfam | PF02664. LuxS. 1 hit. [Graphical view] |
| PIRSF | PIRSF006160. AI2. 1 hit. |
| PRINTS | PR01487. LUXSPROTEIN. |
| ProDom | PD013172. S-ribosylhomocysteinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | LUXS_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PN97 Secondary accession number(s): Q0P958 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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