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A5F9A3 (LUXS_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:VC0395_A0091, VC395_0574
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length172 AA.
Sequence statusComplete.
Protein existenceInferred 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. HAMAP-Rule MF_00091

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00091

Sequence similarities

Belongs to the LuxS family.

Ontologies

Keywords
   Biological processAutoinducer synthesis
Quorum sensing
   LigandIron
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processquorum sensing

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionS-ribosylhomocysteine lyase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

iron ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 172172S-ribosylhomocysteine lyase HAMAP-Rule MF_00091
PRO_1000071261

Sites

Metal binding541Iron By similarity
Metal binding581Iron By similarity
Metal binding1281Iron By similarity

Sequences

Sequence LengthMass (Da)Tools
A5F9A3 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 6D481F831DBB65AF

FASTA17219,081
        10         20         30         40         50         60 
MPLLDSFTVD HTRMNAPAVR VAKTMQTPKG DTITVFDLRF TMPNKDILSE RGIHTLEHLY 

        70         80         90        100        110        120 
AGFMRNHLNG SQVEIIDISP MGCRTGFYMS LIGAPTEQQV AQAWLAAMQD VLKVESQEQI 

       130        140        150        160        170 
PELNEYQCGT AAMHSLEEAK AIAKNVIAAG ISVNRNDELA LPESMLNELK VH 

« Hide

References

[1]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.
[2]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000627 Genomic DNA. Translation: ABQ20738.1.
CP001235 Genomic DNA. Translation: ACP08593.1.
RefSeqYP_001216056.1. NC_009457.1.
YP_002818829.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F9A3.
SMRA5F9A3. Positions 3-161.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A0091.

Proteomic databases

PRIDEA5F9A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ20738; ABQ20738; VC0395_A0091.
ACP08593; ACP08593; VC395_0574.
GeneID5135905.
7774609.
KEGGvco:VC0395_A0091.
vcr:VC395_0574.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1854.
HOGENOMHOG000040371.
KOK07173.
OMARFKQPNQ.
ProtClustDBPRK02260.

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. SSF63411. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLUXS_VIBC3
AccessionPrimary (citable) accession number: A5F9A3
Secondary accession number(s): C3LX83
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families