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Q9RRU8 (LUXS_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
S-ribosylhomocysteine lyase
EC=4.4.1.21
Alternative name(s):
AI-2 synthesis protein
Autoinducer-2 production protein LuxS
Gene names
Name:luxS
Ordered Locus Names:DR_2387
OrganismDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) [Reference proteome] [HAMAP]
Taxonomic identifier243230 [NCBI]
Taxonomic lineageBacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus ›

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceEvidence 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). 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.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the LuxS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 158158S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_0000172218

Sites

Metal binding571Iron
Metal binding611Iron
Metal binding1251Iron

Secondary structure

1 ....................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9RRU8 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 174CC86C50FB714F

FASTA15817,395
        10         20         30         40         50         60 
MPDMANVESF DLDHTKVKAP YVRLAGVKTT PKGDQISKYD LRFLQPNQGA IDPAAIHTLE 

        70         80         90        100        110        120 
HLLAGYMRDH LEGVVDVSPM GCRTGMYMAV IGEPDEQGVM KAFEAALKDT AGHDQPIPGV 

       130        140        150 
SELECGNYRD HDLAAARQHA RDVLDQGLKV QETILLER

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000513 Genomic DNA. Translation: AAF11932.1.
PIRD75280.
RefSeqNP_296108.1. NC_001263.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1INNX-ray1.80A/B1-158[»]
1J6VX-ray2.10A1-158[»]
1VGXX-ray1.90A/B1-158[»]
1VH2X-ray2.00A1-158[»]
1VJEX-ray1.64A/B1-158[»]
ProteinModelPortalQ9RRU8.
SMRQ9RRU8. Positions 7-158.
ModBaseSearch...

Protein-protein interaction databases

STRING243230.DR_2387.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF11932; AAF11932; DR_2387.
GeneID1797935.
KEGGdra:DR_2387.
PATRIC21632492. VBIDeiRad64572_2623.

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040372.
KOK07173.
OMAKAPYVRV.
ProtClustDBPRK02260.

Enzyme and pathway databases

BioCycDRAD243230:GH46-2752-MONOMER.

Family and domain databases

Gene3D3.30.1360.80. 1 hit.
HAMAPMF_00091. LuxS.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFPIRSF006160. AI2. 1 hit.
PRINTSPR01487. LUXSPROTEIN.
ProDomPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF63411. Metalloenz_metal-bd. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9RRU8.

Entry information

Entry nameLUXS_DEIRA
AccessionPrimary (citable) accession number: Q9RRU8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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