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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).

Catalytic activityi

S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = L-homocysteine + (4S)-4,5-dihydroxypentan-2,3-dione.UniRule annotation

Cofactori

Fe cationNote: Binds 1 Fe cation per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi57Iron1
Metal bindingi61Iron1
Metal bindingi125Iron1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Autoinducer synthesis, Quorum sensing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi4.4.1.21. 1856.

Names & Taxonomyi

Protein namesi
Recommended name:
S-ribosylhomocysteine lyaseUniRule annotation (EC:4.4.1.21UniRule annotation)
Alternative name(s):
AI-2 synthesis proteinUniRule annotation
Autoinducer-2 production protein LuxSUniRule annotation
Gene namesi
Name:luxSUniRule annotation
Ordered Locus Names:DR_2387
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001722181 – 158S-ribosylhomocysteine lyaseAdd BLAST158

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi243230.DR_2387.

Structurei

Secondary structure

1158
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 11Combined sources3
Turni14 – 16Combined sources3
Beta strandi19 – 29Combined sources11
Beta strandi35 – 42Combined sources8
Helixi53 – 70Combined sources18
Beta strandi74 – 79Combined sources6
Beta strandi83 – 93Combined sources11
Helixi96 – 111Combined sources16
Turni122 – 124Combined sources3
Turni126 – 129Combined sources4
Helixi133 – 146Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9RRU8.
SMRiQ9RRU8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RRU8.

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4106762. Bacteria.
COG1854. LUCA.
HOGENOMiHOG000040372.
InParanoidiQ9RRU8.
KOiK07173.
OMAiAGFMREH.
OrthoDBiPOG091H0623.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS. 1 hit.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamiPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFiPIRSF006160. AI2. 1 hit.
PRINTSiPR01487. LUXSPROTEIN.
ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63411. SSF63411. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9RRU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDMANVESF DLDHTKVKAP YVRLAGVKTT PKGDQISKYD LRFLQPNQGA
60 70 80 90 100
IDPAAIHTLE HLLAGYMRDH LEGVVDVSPM GCRTGMYMAV IGEPDEQGVM
110 120 130 140 150
KAFEAALKDT AGHDQPIPGV SELECGNYRD HDLAAARQHA RDVLDQGLKV

QETILLER
Length:158
Mass (Da):17,395
Last modified:May 1, 2000 - v1
Checksum:i174CC86C50FB714F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11932.1.
PIRiD75280.
RefSeqiNP_296108.1. NC_001263.1.
WP_010889013.1. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF11932; AAF11932; DR_2387.
GeneIDi1797935.
KEGGidra:DR_2387.
PATRICi21632492. VBIDeiRad64572_2623.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF11932.1.
PIRiD75280.
RefSeqiNP_296108.1. NC_001263.1.
WP_010889013.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliQ9RRU8.
SMRiQ9RRU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_2387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF11932; AAF11932; DR_2387.
GeneIDi1797935.
KEGGidra:DR_2387.
PATRICi21632492. VBIDeiRad64572_2623.

Phylogenomic databases

eggNOGiENOG4106762. Bacteria.
COG1854. LUCA.
HOGENOMiHOG000040372.
InParanoidiQ9RRU8.
KOiK07173.
OMAiAGFMREH.
OrthoDBiPOG091H0623.

Enzyme and pathway databases

BRENDAi4.4.1.21. 1856.

Miscellaneous databases

EvolutionaryTraceiQ9RRU8.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS. 1 hit.
InterProiIPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view]
PfamiPF02664. LuxS. 1 hit.
[Graphical view]
PIRSFiPIRSF006160. AI2. 1 hit.
PRINTSiPR01487. LUXSPROTEIN.
ProDomiPD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF63411. SSF63411. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiLUXS_DEIRA
AccessioniPrimary (citable) accession number: Q9RRU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.