Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q0HLQ3

- LUXS_SHESM

UniProt

Q0HLQ3 - LUXS_SHESM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Shewanella sp. (strain MR-4)
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

Fe cationUniRule annotationNote: Binds 1 Fe cation 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

BioCyciSSP60480:GI2N-964-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:Shewmr4_0934
OrganismiShewanella sp. (strain MR-4)
Taxonomic identifieri60480 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000008079: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 169169S-ribosylhomocysteine lyasePRO_0000298027Add
BLAST

Proteomic databases

PRIDEiQ0HLQ3.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi60480.Shewmr4_0934.

Structurei

3D structure databases

ProteinModelPortaliQ0HLQ3.
SMRiQ0HLQ3. Positions 3-163.
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.

Q0HLQ3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPLLDSFTVD HTRMNAPAVR VAKHMSTPKG DAITVFDLRF CAPNKDILSE
60 70 80 90 100
RGIHTLEHLF AGFMRDHLNG SDVEIIDISP MGCRTGFYMS LIGEPSERQV
110 120 130 140 150
ADAWLASMED VLKVVEQSEI PELNEYQCGT YQMHSLEQAQ DIARNIIAAG
160
VSVNRNDDLK LSDEILGKL
Length:169
Mass (Da):18,847
Last modified:October 3, 2006 - v1
Checksum:i0FC2C06AF4527139
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000446 Genomic DNA. Translation: ABI38014.1.
RefSeqiWP_011621728.1. NC_008321.1.
YP_733071.1. NC_008321.1.

Genome annotation databases

EnsemblBacteriaiABI38014; ABI38014; Shewmr4_0934.
GeneIDi4251865.
KEGGishe:Shewmr4_0934.
PATRICi23578342. VBISheSp133532_0968.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000446 Genomic DNA. Translation: ABI38014.1 .
RefSeqi WP_011621728.1. NC_008321.1.
YP_733071.1. NC_008321.1.

3D structure databases

ProteinModelPortali Q0HLQ3.
SMRi Q0HLQ3. Positions 3-163.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 60480.Shewmr4_0934.

Proteomic databases

PRIDEi Q0HLQ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABI38014 ; ABI38014 ; Shewmr4_0934 .
GeneIDi 4251865.
KEGGi she:Shewmr4_0934.
PATRICi 23578342. VBISheSp133532_0968.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SSP60480:GI2N-964-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MR-4.

Entry informationi

Entry nameiLUXS_SHESM
AccessioniPrimary (citable) accession number: Q0HLQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: October 3, 2006
Last modified: November 26, 2014
This is version 51 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