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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Helicobacter acinonychis (strain Sheeba)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

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

Fe cationUniRule annotationNote: Binds 1 Fe cation per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601IronUniRule annotation
Metal bindingi64 – 641IronUniRule annotation
Metal bindingi127 – 1271IronUniRule annotation

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

BioCyciHACI382638:GJAU-1352-MONOMER.

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:Hac_1463
OrganismiHelicobacter acinonychis (strain Sheeba)
Taxonomic identifieri382638 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000775 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157S-ribosylhomocysteine lyasePRO_0000298001Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi382638.Hac_1463.

Structurei

3D structure databases

ProteinModelPortaliQ17VY9.
SMRiQ17VY9. Positions 7-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiKQPNQDH.
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.

Q17VY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTPNTKMNV ESFNLDHTKV KAPYVRIADR KKGINGDLIV KYDVRFKQPN
60 70 80 90 100
QEHMDMPSLH SLEHLVAEII RNHANYVVDW SPMGCQTGFY LTVLNHDNYT
110 120 130 140 150
EILEVLEKTM QDVLKATEVP ASNEKQCGWA ANHTLEGAKN LAHAFLSKRD

EWSEIGI
Length:157
Mass (Da):17,963
Last modified:July 25, 2006 - v1
Checksum:i3827ED808FAEB261
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260522 Genomic DNA. Translation: CAK00187.1.
RefSeqiWP_011578277.1. NC_008229.1.
YP_665186.1. NC_008229.1.

Genome annotation databases

EnsemblBacteriaiCAK00187; CAK00187; Hac_1463.
KEGGihac:Hac_1463.
PATRICi20586760. VBIHelAci71660_1384.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM260522 Genomic DNA. Translation: CAK00187.1.
RefSeqiWP_011578277.1. NC_008229.1.
YP_665186.1. NC_008229.1.

3D structure databases

ProteinModelPortaliQ17VY9.
SMRiQ17VY9. Positions 7-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi382638.Hac_1463.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAK00187; CAK00187; Hac_1463.
KEGGihac:Hac_1463.
PATRICi20586760. VBIHelAci71660_1384.

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
KOiK07173.
OMAiKQPNQDH.
OrthoDBiEOG68WRBM.

Enzyme and pathway databases

BioCyciHACI382638:GJAU-1352-MONOMER.

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.
ProtoNetiSearch...

Publicationsi

  1. "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a host jump from early humans to large felines."
    Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G., Gressmann H., Achtman M., Schuster S.C.
    PLoS Genet. 2:1097-1110(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sheeba.

Entry informationi

Entry nameiLUXS_HELAH
AccessioniPrimary (citable) accession number: Q17VY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: July 25, 2006
Last modified: April 1, 2015
This is version 53 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.