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Q9RRU8

- LUXS_DEIRA

UniProt

Q9RRU8 - LUXS_DEIRA

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Protein

S-ribosylhomocysteine lyase

Gene
luxS, DR_2387
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - 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).UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 iron ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Iron
Metal bindingi61 – 611Iron
Metal bindingi125 – 1251Iron

GO - Molecular functioni

  1. iron ion binding Source: InterPro
  2. S-ribosylhomocysteine lyase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. quorum sensing Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Autoinducer synthesis, Quorum sensing

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2436-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
S-ribosylhomocysteine lyase (EC:4.4.1.21)
Alternative name(s):
AI-2 synthesis protein
Autoinducer-2 production protein LuxS
Gene namesi
Name:luxS
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
ProteomesiUP000002524: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158S-ribosylhomocysteine lyaseUniRule annotationPRO_0000172218Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi243230.DR_2387.

Structurei

Secondary structure

1
158
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 113
Turni14 – 163
Beta strandi19 – 2911
Beta strandi35 – 428
Helixi53 – 7018
Beta strandi74 – 796
Beta strandi83 – 9311
Helixi96 – 11116
Turni122 – 1243
Turni126 – 1294
Helixi133 – 14614

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 7-158.

Miscellaneous databases

EvolutionaryTraceiQ9RRU8.

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiRDHLNSD.
OrthoDBiEOG68WRBM.

Family and domain databases

Gene3Di3.30.1360.80. 1 hit.
HAMAPiMF_00091. LuxS.
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

MPDMANVESF DLDHTKVKAP YVRLAGVKTT PKGDQISKYD LRFLQPNQGA    50
IDPAAIHTLE HLLAGYMRDH LEGVVDVSPM GCRTGMYMAV IGEPDEQGVM 100
KAFEAALKDT AGHDQPIPGV SELECGNYRD HDLAAARQHA RDVLDQGLKV 150
QETILLER 158
Length:158
Mass (Da):17,395
Last modified:May 1, 2000 - v1
Checksum:i174CC86C50FB714F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE000513 Genomic DNA. Translation: AAF11932.1 .
PIRi D75280.
RefSeqi NP_296108.1. NC_001263.1.
WP_010889013.1. NC_001263.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1INN X-ray 1.80 A/B 1-158 [» ]
1J6V X-ray 2.10 A 1-158 [» ]
1VGX X-ray 1.90 A/B 1-158 [» ]
1VH2 X-ray 2.00 A 1-158 [» ]
1VJE X-ray 1.64 A/B 1-158 [» ]
ProteinModelPortali Q9RRU8.
SMRi Q9RRU8. Positions 7-158.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243230.DR_2387.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF11932 ; AAF11932 ; DR_2387 .
GeneIDi 1797935.
KEGGi dra:DR_2387.
PATRICi 21632492. VBIDeiRad64572_2623.

Phylogenomic databases

eggNOGi COG1854.
HOGENOMi HOG000040372.
KOi K07173.
OMAi RDHLNSD.
OrthoDBi EOG68WRBM.

Enzyme and pathway databases

BioCyci DRAD243230:GH46-2436-MONOMER.

Miscellaneous databases

EvolutionaryTracei Q9RRU8.

Family and domain databases

Gene3Di 3.30.1360.80. 1 hit.
HAMAPi MF_00091. LuxS.
InterProi IPR011249. Metalloenz_LuxS/M16.
IPR003815. S-ribosylhomocysteinase.
[Graphical view ]
Pfami PF02664. LuxS. 1 hit.
[Graphical view ]
PIRSFi PIRSF006160. AI2. 1 hit.
PRINTSi PR01487. LUXSPROTEIN.
ProDomi PD013172. S-ribosylhomocysteinase. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF63411. SSF63411. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  2. "A structural genomics approach to the study of quorum sensing: crystal structures of three LuxS orthologs."
    Lewis H.A., Furlong E.B., Laubert B., Eroshkina G.A., Batiyenko Y., Adams J.M., Bergseid M.G., Marsh C.D., Peat T.S., Sanderson W.E., Sauder J.M., Buchanan S.G.
    Structure 9:527-537(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).

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: September 3, 2014
This is version 90 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

External Data

Dasty 3

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