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Q0I202

- LUXS_HISS1

UniProt

Q0I202 - LUXS_HISS1

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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Histophilus somni (strain 129Pt) (Haemophilus somnus)
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

BioCyciHSOM205914:GJ7V-574-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:HS_0550
OrganismiHistophilus somni (strain 129Pt) (Haemophilus somnus)
Taxonomic identifieri205914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
ProteomesiUP000001970: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168S-ribosylhomocysteine lyasePRO_0000298000Add
BLAST

Proteomic databases

PRIDEiQ0I202.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi205914.HS_0550.

Structurei

3D structure databases

ProteinModelPortaliQ0I202.
SMRiQ0I202. Positions 3-162.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040371.
KOiK07173.
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.

Q0I202-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLLDSFKVD HTRMNAPAVR IAKTMQTPKG DNITVFDLRF CIPNKEILSS
60 70 80 90 100
KGIHTLEHLF AGFMRDHLNN EQVEIIDISP MGCRTGFYMS LIGTPNEQQV
110 120 130 140 150
AEAWLISMQD ILNIKNQDEI PELNEYQCGT YTEHSLEEAQ NIAQNILHRG
160
VGINKNEDLL LDDNLLNS
Length:168
Mass (Da):19,082
Last modified:October 3, 2006 - v1
Checksum:i223733D336B6B852
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000436 Genomic DNA. Translation: ABI24827.1.
RefSeqiYP_718761.1. NC_008309.1.

Genome annotation databases

EnsemblBacteriaiABI24827; ABI24827; HS_0550.
GeneIDi4240033.
KEGGihso:HS_0550.
PATRICi20281065. VBIHaeSom53361_0577.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000436 Genomic DNA. Translation: ABI24827.1 .
RefSeqi YP_718761.1. NC_008309.1.

3D structure databases

ProteinModelPortali Q0I202.
SMRi Q0I202. Positions 3-162.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 205914.HS_0550.

Proteomic databases

PRIDEi Q0I202.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI24827 ; ABI24827 ; HS_0550 .
GeneIDi 4240033.
KEGGi hso:HS_0550.
PATRICi 20281065. VBIHaeSom53361_0577.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci HSOM205914:GJ7V-574-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. "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
    Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
    J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129Pt.

Entry informationi

Entry nameiLUXS_HISS1
AccessioniPrimary (citable) accession number: Q0I202
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 3, 2006
Last modified: October 1, 2014
This is version 50 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