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C4ZYT7

- LUXS_ECOBW

UniProt

C4ZYT7 - LUXS_ECOBW

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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Status
Reviewed - 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

Binds 1 iron ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541IronUniRule annotation
Metal bindingi58 – 581IronUniRule annotation
Metal bindingi128 – 1281IronUniRule annotation

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

BioCyciECOL595496:GI18-2518-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:BWG_2428
OrganismiEscherichia coli (strain K12 / MC4100 / BW2952)
Taxonomic identifieri595496 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001478: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 171171S-ribosylhomocysteine lyasePRO_1000202669Add
BLAST

Proteomic databases

PRIDEiC4ZYT7.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi595496.BWG_2428.

Structurei

3D structure databases

ProteinModelPortaliC4ZYT7.
SMRiC4ZYT7. Positions 3-161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040371.
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.

C4ZYT7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLLDSFTVD HTRMEAPAVR VAKTMNTPHG DAITVFDLRF CVPNKEVMPE
60 70 80 90 100
RGIHTLEHLF AGFMRNHLNG NGVEIIDISP MGCRTGFYMS LIGTPDEQRV
110 120 130 140 150
ADAWKAAMED VLKVQDQNQI PELNVYQCGT YQMHSLQEAQ DIARSILERD
160 170
VRINSNEELA LPKEKLQELH I
Length:171
Mass (Da):19,416
Last modified:July 28, 2009 - v1
Checksum:i131F57F1866DA105
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001396 Genomic DNA. Translation: ACR65571.1.
RefSeqiYP_002927625.1. NC_012759.1.

Genome annotation databases

EnsemblBacteriaiACR65571; ACR65571; BWG_2428.
GeneIDi7954303.
KEGGiebw:BWG_2428.
PATRICi18274302. VBIEscCol60876_2662.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001396 Genomic DNA. Translation: ACR65571.1 .
RefSeqi YP_002927625.1. NC_012759.1.

3D structure databases

ProteinModelPortali C4ZYT7.
SMRi C4ZYT7. Positions 3-161.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 595496.BWG_2428.

Chemistry

BindingDBi C4ZYT7.

Proteomic databases

PRIDEi C4ZYT7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACR65571 ; ACR65571 ; BWG_2428 .
GeneIDi 7954303.
KEGGi ebw:BWG_2428.
PATRICi 18274302. VBIEscCol60876_2662.

Phylogenomic databases

eggNOGi COG1854.
HOGENOMi HOG000040371.
KOi K07173.
OMAi RDHLNSD.
OrthoDBi EOG68WRBM.

Enzyme and pathway databases

BioCyci ECOL595496:GI18-2518-MONOMER.

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

  1. "Genomic sequencing reveals regulatory mutations and recombinational events in the widely used MC4100 lineage of Escherichia coli K-12."
    Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., Wang L.
    J. Bacteriol. 191:4025-4029(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MC4100 / BW2952.

Entry informationi

Entry nameiLUXS_ECOBW
AccessioniPrimary (citable) accession number: C4ZYT7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: October 1, 2014
This is version 35 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