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A4IS03

- LUXS_GEOTN

UniProt

A4IS03 - LUXS_GEOTN

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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Geobacillus thermodenitrificans (strain NG80-2)
Status
Reviewed - Annotation score: 3 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 bindingi55 – 551IronUniRule annotation
Metal bindingi59 – 591IronUniRule annotation
Metal bindingi127 – 1271IronUniRule 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

BioCyciGTHE420246:GIXT-2839-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:GTNG_2762
OrganismiGeobacillus thermodenitrificans (strain NG80-2)
Taxonomic identifieri420246 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
ProteomesiUP000001578: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 158158S-ribosylhomocysteine lyasePRO_0000297998Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi420246.GTNG_2762.

Structurei

3D structure databases

ProteinModelPortaliA4IS03.
SMRiA4IS03. Positions 5-158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040372.
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.

A4IS03-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPSPVESFEL DHCAVKAPYV RHCGVHKIGS DGVVNKFDIR FCQPNKEAMD
60 70 80 90 100
PAAIHTLEHL LAYTLRKHVT KYDHFDIIDI SPMGCQTGFY LVVSGSPTVD
110 120 130 140 150
EIIDLLEETM KDALNATEVP AATERQCGQA KLHDLEAAKE LMRFWLSQEK

SELKKVFG
Length:158
Mass (Da):17,744
Last modified:August 21, 2007 - v2
Checksum:i4507CC34DDC964B9
GO

Sequence cautioni

The sequence ABO68107.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO68107.1. Different initiation.
RefSeqiYP_001126852.1. NC_009328.1.

Genome annotation databases

EnsemblBacteriaiABO68107; ABO68107; GTNG_2762.
GeneIDi4967688.
KEGGigtn:GTNG_2762.
PATRICi21982097. VBIGeoThe136879_2910.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000557 Genomic DNA. Translation: ABO68107.1 . Different initiation.
RefSeqi YP_001126852.1. NC_009328.1.

3D structure databases

ProteinModelPortali A4IS03.
SMRi A4IS03. Positions 5-158.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 420246.GTNG_2762.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABO68107 ; ABO68107 ; GTNG_2762 .
GeneIDi 4967688.
KEGGi gtn:GTNG_2762.
PATRICi 21982097. VBIGeoThe136879_2910.

Phylogenomic databases

eggNOGi COG1854.
HOGENOMi HOG000040372.
KOi K07173.
OrthoDBi EOG68WRBM.

Enzyme and pathway databases

BioCyci GTHE420246:GIXT-2839-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. "Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
    Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
    Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NG80-2.

Entry informationi

Entry nameiLUXS_GEOTN
AccessioniPrimary (citable) accession number: A4IS03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: August 21, 2007
Last modified: November 26, 2014
This is version 46 of the entry and version 2 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