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Q6AAL4

- LUXS_PROAC

UniProt

Q6AAL4 - LUXS_PROAC

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Protein

S-ribosylhomocysteine lyase

Gene

luxS

Organism
Propionibacterium acnes (strain KPA171202 / DSM 16379)
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 bindingi57 – 571IronUniRule annotation
Metal bindingi61 – 611IronUniRule annotation
Metal bindingi124 – 1241IronUniRule 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

BioCyciPACN267747:GHO9-448-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:PPA0450
OrganismiPropionibacterium acnes (strain KPA171202 / DSM 16379)
Taxonomic identifieri267747 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium
ProteomesiUP000000603: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 154154S-ribosylhomocysteine lyasePRO_0000172245Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi267747.PPA0450.

Structurei

3D structure databases

ProteinModelPortaliQ6AAL4.
SMRiQ6AAL4. Positions 4-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LuxS family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1854.
HOGENOMiHOG000040371.
OMAiAANEIQC.
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.

Q6AAL4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAHKMNVESF NLDHTKVAAP FVRVADVKHL PAGDTLTKYD VRFCQPNKEH
60 70 80 90 100
LDMPAVHSLE HSFAECVRNH SDAVIDFGPM GCQTGFYLIM IGEPDVSGTC
110 120 130 140 150
ELVETTLRDI LKLNTTPAAN EVQCGWGANH SIKAAQEAAH TMLNHRDEWE

QVMA
Length:154
Mass (Da):17,114
Last modified:March 15, 2005 - v2
Checksum:i289CB06DE27307C2
GO

Sequence cautioni

The sequence AAT82202.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017283 Genomic DNA. Translation: AAT82202.1. Different initiation.

Genome annotation databases

EnsemblBacteriaiAAT82202; AAT82202; PPA0450.
PATRICi23035561. VBIProAcn64440_0464.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE017283 Genomic DNA. Translation: AAT82202.1 . Different initiation.

3D structure databases

ProteinModelPortali Q6AAL4.
SMRi Q6AAL4. Positions 4-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 267747.PPA0450.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT82202 ; AAT82202 ; PPA0450 .
PATRICi 23035561. VBIProAcn64440_0464.

Phylogenomic databases

eggNOGi COG1854.
HOGENOMi HOG000040371.
OMAi AANEIQC.
OrthoDBi EOG68WRBM.

Enzyme and pathway databases

BioCyci PACN267747:GHO9-448-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. "The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
    Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
    Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: KPA171202 / DSM 16379.

Entry informationi

Entry nameiLUXS_PROAC
AccessioniPrimary (citable) accession number: Q6AAL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: November 26, 2014
This is version 64 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3