A1KW60 (LUXS_NEIMF) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 42.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: S-ribosylhomocysteine lyase EC=4.4.1.21 Alternative name(s): AI-2 synthesis protein Autoinducer-2 production protein LuxS | ||||
| Gene names |
| ||||
| Organism | Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / FAM18) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272831 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › ![]() |
Protein attributes
| Sequence length | 168 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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) By similarity. HAMAP-Rule MF_00091 |
| Catalytic activity | S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione. HAMAP-Rule MF_00091 |
| Cofactor | Binds 1 iron ion per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| 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 | metabolic process Inferred from electronic annotation. Source: GOC quorum sensingInferred from electronic annotation. Source: HAMAP |
| Molecular_function | S-ribosylhomocysteine lyase activity Inferred from electronic annotation. Source: HAMAP iron ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 168 | 168 | S-ribosylhomocysteine lyase HAMAP-Rule MF_00091 | PRO_0000298016 | |||||
Sites | |||||||||
| Metal binding | 54 | 1 | Iron By similarity | ||||||
| Metal binding | 58 | 1 | Iron By similarity | ||||||
| Metal binding | 128 | 1 | Iron By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Meningococcal genetic variation mechanisms viewed through comparative analysis of serogroup C strain FAM18." Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C., Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K., Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S., Quail M.A., Achtman M. Parkhill J.PLoS Genet. 3:230-240(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700532 / FAM18. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM421808 Genomic DNA. Translation: CAM11116.1. |
| RefSeq | YP_975884.1. NC_008767.1. |
3D structure databases | |
| ProteinModelPortal | A1KW60. |
| SMR | A1KW60. Positions 3-162. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 272831.NMC1956. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAM11116; CAM11116; NMC1956. |
| GeneID | 4676172. |
| KEGG | nmc:NMC1956. |
| PATRIC | 20354402. VBINeiMen17609_2429. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1854. |
| HOGENOM | HOG000040371. |
| KO | K07173. |
| OMA | KAPYVRV. |
| ProtClustDB | PRK02260. |
Enzyme and pathway databases | |
| BioCyc | NMEN272831:GJDX-1851-MONOMER. |
Family and domain databases | |
| Gene3D | 3.30.1360.80. 1 hit. |
| HAMAP | MF_00091. LuxS. |
| InterPro | IPR011249. Metalloenz_LuxS/M16. IPR003815. S-ribosylhomocysteinase. [Graphical view] |
| 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] |
| SUPFAM | SSF63411. Metalloenz_metal-bd. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LUXS_NEIMF | ||||||||
| Accession | Primary (citable) accession number: A1KW60 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
